# ad: arcoid location: 2-60.7. origin: Spontaneous. discoverer: Curry, 38a2. references: 1939, DIS 12: 45. phenotype: Wings arched, broad, and somewhat shortened; crossveins close; scutellar groove shallow. Legs may be slightly shorter than wild type. RK3. # add-B: see dmd2 # Additional sex combs: see Asx # ade1: adenosine1 location: 1-57 (right of f). origin: Induced by ethyl methanesulfonate. synonym: ade1-1sd. references: Falk and Nash, 1974, Genetics 76: 755-766. phenotype: Eclosion delayed 2 or 3 days; delay abolished by supplementation of minimal medium with adenosine or guanosine. # ade2 (S. Henikoff and D. Nash) location: 2-17.7 [based on 73 cl-spd recombinants (Keizer, Nash, and Tiong, 1989, Biochem. Genet. 27: 349-53)]. references: Johnstone, Nash, and Naguib, 1985, Biochem. Genet. 23: 539-55. Henikoff, Nash, Hards, Bleskan, Woolford, Naguib, and Patter- son, 1986, Proc. Nat. Acad. Sci. USA 83: 3919-23. Tiong, Keizer, Nash, Bleskan, and Patterson, 1989, Biochem. Genet. 27: 333-48. phenotype: Purine nucleoside auxotroph supplementable with adenine, adenosine, and inosine. Eye color reddish-brown similar to rosy. Lacks detectable levels of the fourth purine de novo synthetic-pathway enzyme, formylglycineamide ribotide amidotransferase (FGARAT; EC 6.33.5.3). Homozygotes and heteroallelic combinations of many alleles have defective wings; the defects include reduced wing size, deranged poste- rior wing margins, and extra wing veins. Macrochaetae are somewhat thinner than normal and reduced in length. ade25, ade26, and ade27 are sterile, perhaps owing to general debil- ity, when homozygous or in heteroallelic combination with one another. Only ade27 was not tested owing to a linked lethal. Most homozygotes and heteroallelic heterozygotes display reduced viability, with the appearance of pharate adults unable to eclose. alleles: allele origin discoverer synonym ref ( comments ___________________________________________________________ ade21 EMS Naguib 2, 3 weak allele ade22 / ray 5 ade23 / ray 5 ade24 / ray 5 ade25 / ray 5 ade26 / ray 5 ade27 / ray 5 ade28 / ray 5 In(2LR)26B; 40-41;57B-C ade29 / ray 5 T(2;3)26B1-2;97D ade210 spont Bryson, 1939 pym1 1, 5 *ade211 spont Neel, 1941 pym2 4 ( 1 = Bryson, 1940, DIS 13: 49; 2 = Henikoff, Nash, Hards, Bleskan, Woolford, Naguib, and Patterson, 1986, Proc. Nat. Acad. Sci. USA 83: 3919-23; 3 = Johnstone, Nash, and Naguib, 1985, Biochem. Genet. 23: 539-55; 4 = Neel, 1942, Am. Nat. 76: 630-34; 5 = Tiong, Keizer, Nash, Bleskan, and Patterson, 1989, Biochem. Genet. 27: 333-48. cytology: Placed in 26B, probably 26B1-2, based on breakpoints common to In(2LR)ade8 = In(2LR)26B;40-41;57B-C and T(2;3)ade9 = T(2;3)26B1-2;97D. Also included in Df(2L)ade2-1 = Df(2L)25F;26B5-6, Df(2L)ade2-2 = Df(2L)25F2-3;26D-E, and Df(2L)ade2-3 = Df(2L)26A;26B5-6. # ade3 (S. Henikoff and D. Nash) location: 2-20. origin: Induced by ethyl methanesulfonate. discoverer: Nash. synonym: Gart. references: Johnstone, Nash, and Naguib, 1985, Biochem. Genet. 23: 539-55. Henikoff, Nash, Hards, Bleskan, Woolford, Naguib, and Patter- son, 1986a, Proc. Nat. Acad. Sci. USA 83: 3919-23. Henikoff, Keene, Sloan, Bleskan, Hards, and Patterson, 1986b, Proc. Nat. Acad. Sci. USA 83: 720-24. phenotype: Purine nucleoside auxotroph supplementable with adenine, adenosine, and inosine. Recovery of ade3 progeny from crosses between ade3 and ade3/SM5 is about 1% when raised on minimal medium. Less than 3% of the normal activity purine de novo synthetic pathway enzyme, glycineamide ribotide transformylase [EC 2.1.2.2 (GART)]. Eye color normal. cytology: 27C by means of in situ hybridization of cloned sequence. molecular biology: Corresponds to the cloned sequence selected by Henikoff, Keene, Tatchell, Hall, and Nasmyth [1981, Nature (London) 289: 37] by its ability to complement ade8 in yeast, which codes for GART. Seven exons specify a 4.7 kb mRNA encoding the second, third, and fifth de novo purine biosynthetic-pathway enzyme activities, glycineamide ribotide synthetase [EC 6.3.4.13 (GARS)], aminoimidazole ribotide syn- thetase [EC 6.3.31 (AIRS)], and GART, on a 1353 amino-acid polypeptide. The first four exons also specify a 1.7 kb mRNA encoding Gars alone on a 434 amino acid polypeptide (Henikoff et al.). This smaller polypeptide is identical to the NH2- terminal portion of the larger, except for the last amino acid, as a consequence of alternative processing of the pri- mary transcript. The ade3 mutation is a single base transi- tion changing a conserved glycine (found at that position in yeast ade8) to a serine at amino acid 1164 of the large polypeptide. A functional pupal cuticle protein gene is found within the first intron (interrupting the GARS domain), is encoded on the other DNA strand, and is itself interrupted by a single intron between codons 4 and 5 of a 184 amino-acid open reading frame. This intronic gene (Pcp) is expressed primarily in abdominal epidermal cells that secrete the pupal cuticle (Henikoff, Keene, Fechtel, and Fristrom, 1986, Cell 44: 33-42) Adenine phosphoribosyl transferase: see Aprt # Adenylate kinase C: see Adk-C # Adh: Alcohol dehydrogenase (M. Ashburner) location: 2-50.1. references: Johnson and Denniston, 1964, Nature (London) 204: 906-07. Grell, Jacobson, and Murphy, 1965, Science 149: 80-82. Ursprung and Leone, 1965, J. Exp. Zool. 160: 147-54. phenotype: Structural gene for alcohol dehydrogenase [ADH (EC 1.1.1.1)]. Natural populations are polymorphic for three electrophoretic alleles (AdhF, AdhS, AdhF-ChD) and for three rarer electrophoretic alleles (AdhUS, AdhF', AdhUF). The fre- quency of the AdhF allele increases, at the expense of AdhS, with increasing latitude in both northern and southern hemi- spheres [Johnson and Schaffer, 1973, Biochem. Genet. 10: 149-63; Vigue and Johnson, 1973, Biochem. Genet. 9: 213-27; Wilks, Gibson, Oakeshott and Chambers, 1980, Aust. J. Biol. Sci. 33: 575-85; Anderson, 1981, Genetic Stu- dies of Drosophila Populations (Gibson and Oakes, eds.). Aus- tralian National University Press, pp. 237-50; Anderson and Chambers, 1982, Evolution 36: 86-96]. Confers resistance to ethanol; flies lacking ADH rapidly become intoxicated and eventually die on exposure to ethanol (Grell, Jacobson and Murphy, 1968, Ann. N.Y. Acad. Sci 151: 441-45; Vigue and Sofer, 1976, Biochem. Genet. 14: 127-135; David, Bocquet, Arens and Fouillet, 1976, Biochem. Genet. 14: 989-97). However, ethanol sensitivity is complex since even Adh nulls are more resistant to ethanol when young than when old (Vigue and Sofer, 1976; Tsubota). Adh+ flies are killed by low concentrations of unsaturated secondary alcohols (e.g. 1-penten-3-ol; 1-pentyn-3-ol) but not by unsaturated primary alcohols (e.g. 1-penten-1-ol) (Sofer and Hatkoff, 1972, Genetics 72: 545-49), presumably due to the formation of toxic ketones. This allows the chemi- cal selection of Adh nulls (Sofer and Hatkoff, 1972; O'Donnell, Gerace, Leister and Sofer, 1975, Genetics 79: 73- 83). ADH may play a metabolic role independent of alcohol detoxication, i.e. in the metabolism of higher alcohols (see Winberg, Thatcher and McKinley-McKee, 1982, Biochem. Biophys. Acta 704: 7-16). ADH also catalyses the oxidation of acetal- dehyde to acetate (Heinstra, Eisses, Schoonen, Aben, de Winter, van de Horst, van Marrewijk, Beenakkers, Scharloo and Thorig, 1983, Genetica 60: 129-37; Moxon, Holmes, Parsons, Irving, and Doddrell, 1985, Comp. Biochem. Physiol. 80B: 525-35). Specific activity of ADH changes with development, with peaks at the end of the third larval instar and about four days after eclosion (Ursprung, Sofer and Burroughs, 1970, Wilhelm Roux's Arch. Entwicklungsmech. Org. 164: 201-08; Dunn, Wilson and Jacobson, 1969, J. Exp. Zool. 171: 185-90; Leibenguth, Rammo and Dubiczky, 1979, Wilhelm Roux's Arch. Dev. Biol. 187: 81-88; Maroni and Stamey, 1983, DIS 59: 77- 79; Anderson and McDonald, 1981, Canad. J. Genet. Cytol. 23: 305-13). Most of the activity is in the larval fat body and gut and the adult fat body (Ursprung, Sofer and Bur- roughs). Maternal inheritance of ADH by embryos and larvae (O'Donnell et al.; Leibenguth et al.). Half life of ADH-F in vivo estimated as 55.3 hours (Anderson and McDonald, 1981, Biochem. Genet. 19: 411-19). Not expressed in SL2 tissue culture cells, but transfected cloned gene is (Benyajati and Dray, 1984, Proc. Nat. Acad. Sci. 1701-05). Ethanol tolerance usually correlated with ADH activity and polymorphic experimental populations exposed to ethanol usu- ally show an increase in the frequency AdhF (McDonald and Avise, 1976, Biochem. Genet. 14: 347-55; Cavener and Clegg, 1978, Genetics 90: 629-44; van Delden, Kamping and van Dijk, 1975, Experientia 31: 418-19; Oakeshott, Gibson, Anderson and Champ, 1980, Aust. J. Biol. Sci. 33: 105-14; McDonald, Chambers, David and Ayala, 1977, Proc. Nat. Acad. Sci. USA 74: 4562-66). Flies carrying AdhF tend to be more resistant than those carrying only AdhS to ethanol [Kamping and van Del- den, 1978, Biochem. Genet. 16: 541-55; Ainsley and Kitto, 1975, Isozymes (C. Markert, ed.). Academic Press, Vol. II, pp. 733-43; Briscoe, Robertson and Malpica, 1975, Nature (Lon- don) 253: 148-49]. Electrophoresis of homozygous genotypes usually reveals three interconvertable isozymes [Ursprung and Leone; Johnson and Denniston; Grell et al., 1965; Ursprung and Carlin, 1968, Ann. N.Y. Acad. Sci. 151: 456-75; Jacobson, Murphy and Hart- mann, 1970, J. Biol. Chem. 245: 1075-83; Jacobson and Pfuderer, 1970, J. Biol. Chem. 245: 3938-44; Jacobson, Murphy and Ortiz, 1972, Arch. Biochem. Biophys. 149: 22-35; Knopp and Jacobson, 1972, Arch. Biochem. Biophys. 149: 36-41; Schwartz, Gerace, O'Donnell and Sofer, 1975, Isoenzymes (C. Markert, ed.). Academic Press, Vol. I, pp. 725-51]. These vary in activity and stability, the most cathodal being more active, but less stable, than the more anodal forms. They probably result from the binding of 0, 1 or 2 moles per mole of a NAD+ addition complex with a carbonyl compound [Schwartz and Sofer, 1976, Nature (London) 263: 129-31; Schwartz, O'Donnell and Sofer, 1979, Arch. Biochem. Biophys. 194: 365- 78; Winberg, Thatcher and McKinley-McKee, 1983, Biochem. Genet. 21: 63-80]. Feeding flies acetone, propan-2-ol, or 3-hydroxy-butanone, for example, converts isozymes to most anodal form and results in loss of enzyme activity in vitro and in vivo (Schwartz and Sofer, 1976; Papel, Henderson, van Herrewege, David and Sofer, 1979, Biochem. Genet. 17: 533- 63). ADH has been purified (Sofer and Ursprung, 1968, J. Biol. Chem. 243: 3118-25; Schwartz et al., 1975; Thatcher, 1977, Biochem. J. 163: 317-23; Leigh Brown and Lee, 1979, Biochem. J. 179: 479-82; Juan and Gonzalez-Duarte, 1980, Biochem. J. 189: 105-10; Elliot and Knopp, 1975, Methods Enzymol. 41: 374-79; Chambers, 1984, Biochem. Genet. 22: 529-50). It is a homodimer with monomeric subunit molec- ular weight of 27500 daltons (Thatcher, 1980, Biochem. J. 187: 875-83); molecular extinction coefficient 4.8 X 104 liter/mol/cm (Juan and Gonzalez-Duarte, for ADH-S). Complete amino acid sequence determined by Thatcher (1980; see also Schwartz and Jornvall, 1976, Europ. J. Biochem. 68: 159-68; Auffret, Williams and Thatcher, 1978, FEBS Lett. 90: 324-26; Benyajati, Place, Powers, and Sofer, 1981, Proc. Nat. Acad. Sci. USA 78: 2317-21; Chambers, Laver, Campbell and Gibson, 1981, Proc. Nat. Acad. Sci. USA 78: 3103-07) with secondary structure predictions (Thatcher and Sawyer, 1980, Biochem J. 187: 884-86; Benyajati et al., 1981). Limited homology in supposed catalytic region with ribitol dehydrogenase of Kleb- siella (Jornvall, Persson and Jeffry, 1981, Proc. Nat. Acad. Sci. USA 78: 4226-30). ADH shows a broad substrate specificity but is more active (by at least a factor of 5) with secondary than primary alcohols and shows highest activity to 3-6 carbon alcohols (Sofer and Ursprung; Thatcher and Camfield, 1977, Winberg et al., 1982, Chambers et al.). Differences in substrate speci- ficity, kinetic constants and stability of different electro- phoretic variants often reported (Anderson and McDonald, 1983, Proc. Nat. Acad. Sci. USA 80: 4798-802). Considerable hetero- geneity in the specific activity of ADH within and between different AdhF and AdhS strains, though AdhS strains tend to be lower than AdhF [Day, Hillier and Clarke, 1974, Biochem. Genet. 11: 141-53, 155-65; Day and Needham, 1974, Biochem. Genet. 11: 167-75; Gibson, 1970, Nature (London) 227: 959- 61; Gibson, Chambers, Wilkes and Oakeshott, 1980, Aust. J. Biol. Sci. 33: 479-89; Gibson and Miklovitch, 1971, Experien- tia 27: 99-100; Kreitman, 1980, Genetics 95: 467-75; Oak- eshott, 1976, Aust. J. Biol. Sci. 29: 365-73; Sampsell, 1977, Biochem. Genet. 15: 971-88; Sampsell and Sims, 1982, Nature (London) 296: 853-55; Thorig, Schoone and Scharloo, 1975; Biochem. Genet. 13: 721-31; Vigue and Johnson; Hewitt, Pip- kin, Williams and Chakrabartty, 1974, J. Hered. 65: 141-44; Ward, 1974, Biochem. Genet. 12: 449-58; Ward, 1975, Genet. Res. 26: 81-93; Maroni, Laurie-Ahlberg, Adams and Wilton, 1982, Genetics 101: 431-66; Rasmuson, Nilson and Zeppezauer, 1966, Hereditas 56: 313-16; Clarke, Camfield, Garvin and Pitts, 1979, Nature (London) 180: 517-18; Laurie-Ahlberg, Maroni, Bewley, Lucchesi and Weil, 1980, Proc. Nat. Acad. Sci. USA 77: 1073-77; Barnes and Birley, 1978, Heredity 40: 51- 57; Barnes and Birley, 1978, Biochem. Genet. 16: 155-65; McDonald and Ayala, 1978, Genetics 89: 371-88; McDonald et al., 1980; Lewis and Gibson, 1978, Biochem. Genet. 16: 159- 70]. With the exception of the studies by Thatcher and Sheik (1981, Biochem. J. 197: 111-17), Winberg et al. (1982), McDonald, Anderson and Santos (1980, Genetics 95: 1013-22); Eisses, Schoonen, Aben, Scharloo, and Thorig (1985, Mol. Gen. Genet. 199: 76-81) and Moxon et al. (1985), these were all done with crude extracts and not purified enzyme. Thatcher and Sheikh find the relative thermostabilities to be ADH-S > ADH-F > ADH-n5 > ADH-D. ADH-S shows slower dissociation of NADH from NADN-enzyme complex than ADH-F (Winberg, Hovik, and McKinley-McKee, 1985, Biochem. Genet. 23: 205-16). ADH is not a metalloenzyme (Place, Powers and Sofer, 1980, Fed. Proc. 39: 1640); but, paradoxically, is inhibited by certain metal ion chelators, e.g. pyrazole (Place, Powers and Sofer; Winberg et al., 1982; Moxon et al., 1985). Utilization of ethanol as an energy source (van Herrewege and David, 1974, C. Rend. Acad. Sci. Paris 279D: 335-38; van Herrewege, David and Grantham, 1980, Experientia 36: 846-47; Libion-Mannaert, Delcour, Deltombe-Lietaert, Lenelle-Montfort and Elens, 1976, Experentia 32: 22-23) depends on ADH activity (David, Bocquet, van Herrewege, Fouillet and Arens, 1978, Biochem. Genet. 16: 203-11). AdhF homozygotes usually show a better ability to survive on ethanol as a sole energy source than AdhS homozygotes (Daly and Clarke, 1981, Heredity 46: 219-26; Anderson, McDonald and Santos, 1981, Experientia 37: 463-64). AdhF and AdhS homozygotes also show behavioural differences in their response to ethanol (Parsons, 1977 Oecologia 30: 141-46; Cavener, 1979, Behav. Genet. 9: 359- 65; Gelan and McDonald, 1980, Behav. Genet. 10: 237-49; Hougonto, Lietaert, Libion-Mannaert, Feytmans and Elens, 1982, Genetica 58: 121-28; Parsons, 1980, Behav. Genet. 10: 183- 90; Parsons, 1980, Experientia 36: 1070-71). D. simulans enzyme monomers form heterodimers with those of D. melanogaster (E.H. Grell); D. simulans enzyme purified (Juan and Gonzalez-Duarte, 1981, Biochem. J. 195: 61-69). Sequence of D. simulans ADH (from DNA) similar to that of AdhS with following changes: ser1 -> ala1; gln82 -> lys82; ile184 -> val184 (Bodmer and Ashburner, 1984, Nature 309: 425-30). D. simulans and D. melanogaster enzymes differentially regu- lated in hybrids (Dickenson, Rowan, and Brennan, 1984, Hered- ity 52: 215-25). The Adh genes from D. orena and D. mauri- tiana have also been sequenced (Bodmer and Ashburner), and those of D. erecta, D. teissieri and D. yakuba mapped with restriction enzymes (Langley, Montgomery and Quattlebaum, 1982, Proc. Nat. Acad. Sci. USA 79: 5631-35). alleles: Large numbers of alleles have been selected and characterized. This information is summarized in the follow- ing tables: The first table describes the origins and pheno- types of the electrophoretic variants, the majority of which were isolated from natural populations; the second describes the origins and phenotypes of the null alleles; In addition 16 isolations of null alleles from four Australian locations have been described (Freeth and Gibson, 1985, Heredity 55: 369-74); not clear how many mutational events represented. _____________________________________________________________________________________________________________________ allele origin source discoverer ref ( migration | thermo rate (pI) stability _____________________________________________________________________________________________________________________ Adh71k / spont Thorig 5, 6, 13, 22 (6.4) > AdhF AdhA1 ` recomb. Adhn1/Adhn5 Maroni 13, 15 (7) < AdhS AdhB7 ` recomb. Adhn1/Adhn5 Maroni 13, 15 (7) < AdhS AdhD EMS AdhF Grell 9, 19 (6) AdhF spont Johnson and 1, 7, 12, 16, 20 6.4 Denniston AdhF' spont (Congo) David 4, 17, 20 6.5 AdhF(o) / - spont Eisses 6 (6.4) > AdhF AdhF-ChD - spont Lewis 2, 3, 8, 14, 24 (6.4) > AdhF; > AdhS AdhFm spont Sampsell 18 (6.4) AdhFr - spont Sampsell 13, 18 (6.4) > AdhF AdhFs spont Sampsell 13, 18 (6.4) < AdhF AdhI spont Ursprung 11, 23 (6.4) and Leone AdhII n spont Ursprung 11, 23 (7) and Leone AdhS spont Johnson and 7 Denniston AdhSm n spont Sampsell 18 (7) AdhSs spont Sampsell 13, 18 (7) < AdhF AdhUF spont 20, 21 6.0 AdhUS spont (Congo) David 4, 10, 20 7.8 ( 1 = Benyajati, Place, Powers, and Sofer, 1981, Proc. Nat. Acad. Sci. USA 78: 2717-21; 2 = Chambers, Laver, Campbell, and Gibson, 1981, Proc. Nat. Acad. Sci. USA 78: 3103-07; 3 = Chambers, Wilks, and Gibson, 1981, Aust. J. Biol. Sci. 34: 625-37; 4 = David, 1978, Recherche 9: 482-83; 5 = Eisses, Schoonen, Scharloo, Thorig, 1985, Comp. Biochem. Physiol. 82: 863-68. 6 = Eisses, Thorig, and Scharloo, 1981, Genetics 97: s33; 7 = Fletcher, Ayala, Thatcher, and Chambers, 1978, Proc. Nat. Acad. Sci. USA 75: 5609-12; 8 = Gibson, Chambers, Wilkes, and Oakeshott, 1980, Aust. J. Biol. Sci. 33: 479-89; 9 = Grell, Jacobson, and Murphy, 1968, Ann. NY Acad. Sci. 151: 441-55; 10 = Grossman, Koreneva, and Ulitscaya, 1970, Genetika (Moscow) 6(2): 91- 96; 11 = Hewitt, Pipkin, Williams, and Chakrabartty, 1974, J. Hered. 65: 141-48; 12 = Johnson and Denniston, 1964; Nature (London) 204: 906-07; 13 = Kreitman, 1980, Genetics 95: 467-75; 14 = Lewis and Gibson, 1978, Biochem. Genet. 16: 159-70; 15 = Maroni, 1978, Biochem. Genet. 16: 509-23; 16 = Retzios and Thatcher, 1979, Biochemie 61: 701-04; 17 = Retzios and Thatcher, 1980, Biochem. Soc. Trans. 9: 298-99; 18 = Sampsell, 1977, Biochem. Genet. 15: 971- 88; 19 = Schwartz and Jornvall, 1976, Europ. J. Biochem. 68: 159-68; 20 = Thatcher, 1980, Biochem. J. 187: 875-83; 21 = Thatcher and Camfield, 1977, Biochem. Soc. Trans. 5: 271-72; 22 = Thorig, Schoone, and Scharloo, 1977, Biochem. Genet. 13: 721-731; 23 = Ursprung and Leone, 1965, J. Exp. Zool. 160: 147-54; 24 = Wilks, Gibson, Oakeshott, and Chambers, 1980, Aust. J. Sci. 33: 375-85. | Numbers in parentheses inferred from phenotypic description; others represent actual measurements (Thatcher, 1980, Biochem J. 187: 875-83). / Unlike AdhF, will oxidize dihydroorotic acid to orotic acid and sarcosine to glycine. ` Probably identical. - Probably the same as Adh71k. = AdhF. n = AdhS. ______________________________________________________________________________________________________________________________________ derivative forms active allele origin ( of discoverer ref | activity CRM hybrid enzyme notes ______________________________________________________________________________________________________________________________________ Adhfn4 formaldehyde AdhD Sofer 2-4, 9 - - Adhfn6 formaldehyde AdhD Sofer 2-4, 9 - - Adhfn23 formaldehyde AdhD Sofer 2-4, 9 - + / Adhfn24 formaldehyde AdhD Sofer 2-4, 9 - - Adhn1 EMS AdhS E.H. Grell 6, 7, 10, 14 20% + + ` Adhn2 EMS AdhS E.H. Grell 6, 7, 10, 14 - 5% - Adhn3 EMS AdhS E.H. Grell 6, 7, ,10, 14 - 15% - Adhn4 EMS AdhD E.H. Grell 6, 7, 10, 14 - - Adhn5 EMS AdhD E.H. Grell 6, 12-14, 17, 18 leaky ts + - Adhn6 EMS AdhF Gerace 5, 9, 14 - 44% - Adhn7 EMS AdhF Gerace 5, 9, 14 - 54% - Adhn8 EMS AdhF Gerace 5, 9, 14 - 61% - Adhn9 EMS AdhF Gerace 5, 9, 14 - 71% - Adhn10 EMS AdhF Gerace 5, 9, 14 - - Adhn11 EMS AdhF Sofer 9-12, 13, 0.02% 27% + 14-17 Adhn12 EMS AdhF Sofer 9, 10, 14 - 73% - Adhn13 EMS AdhF Sofer 9, 10, 14 - 5% - Adhn14 EMS AdhF Sofer 9, 10, 14 - - Adhn967 spont 18 n AdhnA EMS CyO, AdhF Sofer 5, 14 - - AdhnB EMS CyO, AdhF Sofer 5, 14 - + - AdhnC1 EMS AdhUF Ashburner AdhnC2 EMS AdhUF Ashburner leaky ts AdhnLA2 X ray AdhF Aaron 1, 8 - + i AshnLA73 X ray AdhF Aaron 1, 8 - - AdhnLA74 X ray AdhF Aaron 1, 8 - + AdhnLA80 X ray AdhF Aaron 1, 8 - + k AdhnLA248 X ray AdhF Aaron 1, 8 - - AdhnLA249 X ray AdhF Aaron 1, 8 - + AdhnLA252 X ray AdhF Aaron 1, 8 - + AdhnLA319 spont AdhD Aaron 1, 8 - + AdhnLA378 X ray AdhF Aaron 1, 8 - AdhnLA405 X ray AdhF Aaron 1, 8 - + i ( Adhfn4 - Adhfn24 and Adhn11 - Adhn14 selected as larvae on pentenol; Adhn6 - Adhn10, AdhnA, AdhnB, and the AdhnLA series of alleles selected as adults on pentenol. | 1 = Aaron, 1979, Mutat. Res. 63: 127-37; 2 = Benyajati, Place, Powers, and Sofer, 1981, Proc. Nat. Acad. Sci. USA 78: 2717-21; 3 = Benyajati, Place, and Sofer, 1983, Mutat. Res. 111: 1-7; 4 = Benyajati, Place, Wang, Pentz, and Sofer, 1982, Nucleic Acids Res. 10: 7261-72; 5 = Gerace and Sofer, 1972, DIS 49: 39; 6 = Grell, Jacobson, and Murphy, 1968, Ann. N.Y. Acad. Sci. 151: 441-55; 7 = Kamping and van Delden, 1980, DIS 55: 89; 8 = Kelley, Mims, Farnet, Dicharry, and Lee, 1985, Genetics 109: 365- 77; 9 = O'Donnell, Gerace, Leister, and Sofer, 1975, Genetics 79: 73-83; 10 = Pelliccia and Sofer, 1982, Biochem. Genet. 20: 297-313; 11 = Reddy, Pelliccia, and Sofer, 1980, Biochem. Genet. 18: 339-51; 12 = Sampsell, 1977, Biochem. Genet. 15: 971-88; 13 = Schwartz and Jorn- vall, 1976, Europ. J. Biochem. 68: 159-68; 14 = Schwartz and Sofer, 1976, Genetics 83: 126-36; 15 = Thatcher, 1980, Biochem. J. 187: 875-83; 16 = Thatcher and Retzios, 1980, Protides of Biol. Fluids 28: 157-60; 17 = Thatcher and Sheikh, 1981, Biochem. J. 197: 111-17; 18 = Vigue and Sofer, 1974, Biochem. Genet. 11: 387-96. / Polypeptide smaller than wild type. ` Polypeptide slightly larger than wild type on SDS gels and electrophoretic mobility altered on non-denaturing gels. - Purified enzyme thermolabile; Adhn5 flies grown at 18 show loss of both ADH activity and CRM following a shift to 30 (Tsubota); recovery on return to 18 takes several days (Vigue and Sofer; Tsubota). Mutation in adenine ribose pocket of coenzyme binding domain; is not bound to 5 -AMP sepharose and cannot recog- nize NAD+ (Thatcher and Retzios), AdhF/Adhn11 forms an active dimer that migrates as AdhF/AdhUF (Schwartz and Jorn- vall; Schwartz and Sofer, Pelliccia and Sofer). Shows weak intracistronic complementation with Adhn6 Adhn7 Adhn12 and AdhnA (Thatcher; Reddy et al.). Adhn6/Adhn11 heterozygotes display partial resistance to alcohol; hybrid enzyme activity heat labile; displays altered substrate binding properties (Pelliccia and Couper, 1984, DIS 60: 160-62). n Isolated from natural population. - Polypeptide shorter than normal (24 kilodaltons). i In vitro translation product of mRNA smaller than that of wild type (Pelham and Bodmer). k Protein unstable by two-dimensional gel electrophoretic analysis. cytology: Placed in 35B3 by in situ hybridization. molecular biology: Structural gene cloned (Goldberg, 1980, Proc. Nat. Acad. Sci. USA 77: 5794-98) and sequenced [Gold- berg; Benyajati et al., 1981; Haymerle, 1983, Thesis, Univer- sity of Cambridge; Kreitman, 1983, Nature (London) 304: 412- 17; Benyajati, Place, Wang, Pentz, and Sofer, 1982, Nucleic Acids Res. 10: 7261- 72]. Partial sequence (3' end) of cDNA clone by Benyajati, Wang, Reddy, Weinberg and Sofer (1980, Nucleic Acids Res. 8: 5649- 67). Variation in restriction enzyme sites within and around Adh (Langley et al.). AdhF alleles are polymorphic for insertion substitution changes within the 5' non-coding region intron (Kreitman, 1983). Sequence comparisons between 5' flanking regions and exons in D. melanogaster and D. simulans indicate excess polymorphism in the D. melanogaster 5' flanking region (Kreitman and Aguade, 1986, Genetics 114: 93-100; Aquadro, Desse, Blond, Langley, and Laurie-Ahlberg, 1986, Genetics 114: 1165-90). Standard amino acid sequence taken to be that of ADH-S (Thatcher, 1980 with two corrections: glu25 (not gln) and an extra tryptophan at 251 (Benyajati et al., 1981). Standard DNA sequence is that of AdhS allele from clone pSAC1 of Gold- berg (Benyajati et al., 1981, 1982, 1983; Haymerle); numbered from -1/+1, +1 being the 'A' of the ATG initiating codon. All changes with respect to coding strand. Two primary transcripts: major larval transcript initiated from -69, 24 bp from a TATA box (-100 to -94); major adult transcript initiated from -766, 24 bp from a TATA box (-808 to -800). The major adult transcript is processed by the removal of an intervening sequence between -689 and -36. There are two introns within the coding sequence, from +100 to +164 and from +571 to +639. The polyA addition site is from +1028 to +1034 and the 3' end of the mRNA at +1079. (Benyajati et al., 1981, 1983, Henikoff, 1983, Nucleic Acids Res. 11: 4735-52). An 11.8 kb SacI restriction fragment of the AdhF allele shown by P-element-mediated germline transformation to contain all cis-acting DNA sequences necessary for correct expression (quantitative levels of mRNA and enzyme; tissue specificity; developmental switch in promoter usage)(Goldberg, Posakony, and Maniatis, 1983, Cell 34: 59-73. In vitro recombinants rule out the 5' flanking sequences as responsible for the two- to threefold higher enzyme activity and increased amount of ADH protein in AdhF compared to AdhS; the only consistent differences are at three nucleotide positions, one at 1490 responsible for the electrophoretic difference and two silent third-codon substitutions at nucleotides 1443 and 1527 (Laurie-Ahlberg and Stamm, 1987, Genetics 115: 129-40); increase probably not attributable to increased levels of mRNA (Laurie and Stamm, 1988, Proc. Nat. Acad. Sci. USA 85: 5161- 65). Transcript of Drosophila gene transfected into yeast spliced normally (Watts, Castle, and Beggs, 1983, EMBO J. 2: 2085-91). A fusion of Adh to the Hsp70 promoter has been inserted into a P element and used in transformation experi- ments in Adh deficient flies; in such transformants Adh+ func- tion is under heat-shock control (Bonner, Parks, Parker- Thornberg, Mortin and Pelham, 1984, Cell 37: 979-91). Molecu- lar information on alleles in following table. ______________________________________________________________________ allele molecular biology ref ( ______________________________________________________________________ Adh71k lys 192 -> thr 192; pro 214 -> ser 214 7 AdhD lys 192 -> thr 192; gly 232 -> glu 232 10, 12 AdhF lys 192 -> thr 192; A713 -> C713 1, 10, 11, 14 AdhF' ala 51 -> glu 51 10 AdhF-ChD lys 192 -> thr 192; pro 214 -> ser 214 4 Adhfn4 No mature mRNA; 16 bp deletion in 2, 3 first intron (146-162); AG(163-164) splice acceptor changed to GG splicing defective. Adhfn6 No mature mRNA; 6 bp deletion in 2, 3 first intron (106-111); 101-105 substituted by CGATC; splicing defective. Adhfn23 34 bp deletion in 3 coding region 2, 3 (724-758); read through of normal termination triplet. Adhfn24 50% wild-type mRNA level; 2, 3 11 bp deletion in second exon (256-266); Premature chain termination Adhn4 C312 -> T312; gln 83 -> ter 83 2, 3 Destroys Pvu II site (Chia) Adhn11 gly 14 -> asn 14 10, 12, 13 AdhnB UGG -> UGA 8, 9 in trp 234 codon; suppressible in vitro with yeast ochre suppressor tRNA AdhnLA248 250 bp insertion formed by 5, 6 unequal crossover between exon 3 (at +708) and exon 2 (at +465) with 7bp (GTGCAAC) inserted at the junction. AdhS standard nucleotide sequence 1, 2, 3, 10, 13 AdhUF asn8 -> ala8; ala45 -> asp45; 10, 13, 14 lys 192 -> thr 192 AdhUS lys 192 unchanged 11 ( 1 = Benyajati, Place, Powers, and Sofer, 1981, Proc. Nat. Acad. Sci. USA 78: 2717-21; 2 = Benyajati, Place, and Sofer, 1983, Mutat. Res. 111: 1-7; 3 = Benyajati, Place, Wang, Pentz, and Sofer, 1982, Nucleic Acids Res. 10: 7261- 72; 4 = Chambers, Laver, Campbell, and Gibson, 1981; Proc. Nat. Acad. Sci. USA 78: 3103-07; 5 = Chia, Karp, McGill, and Ashburner, 1985, J. Mol. Biol. 186: 689-706; 6 = Chia, Savakis, Karp, Pelham, and Ashburner, 1985, J. Mol. Biol. 186: 679-88; 7 = de Boer, Andriesse, and Weisbeek; 8 = Kubli, Schmidt, Martin, and Sofer, 1982, Nucleic Acids Res. 10: 7145-52; 9 = Martin, Place, Pentz, and Sofer, 1985, J. Mol. Biol. 184: 221-29; 10 = Retzios and Thatcher, 1979, Biochimie 61: 701-04; 11 = Retzios and Thatcher, 1980, Biochem. Soc. Trans. 9: 298-99; 12 = Schwartz and Jornvall, 1976, European J. Biochem. 68:: 159-68; 13 = Thatcher, 1980, Biochem. J. 187: 875-83; 14 = Thatcher and Camfield, 1977, Biochem. Soc. Trans. 5: 271-72. # adl: see l(1)adl # adp60: adipose location: 2-83.4. origin: Spontaneous. discoverer: Doane, 1960. references: 1961, DIS 35: 78. 1963, DIS 38: 32. 1963, Proc. 23rd Ann. Biol. Coll., Oregon State Univ. Press, Corvallis, pp. 65-88. 1969, J. Exp. Zool. 171: 321-42. phenotype: Adult fat body hypertrophies as cells become dis- torted by enormous oil globules. Lipid accumulated at expense of glycogen in fat body; yolk deposition retarded (Doane, 1963, DIS 37: 73-74; Doane, 1980, Evolution 34: 868-74). Lipid content and fatty acid profiles compared for various developmental stages in adp60 and wild type (Teague, Clark, and Doane, 1986, J. Exp. Zool. 240: 95-104). Abnormal fat bodies visible through body wall of 6-day-old and older adults when submerged in 95% alcohol and then water. Corpus allatum of mated females hypertrophies. Females fertile but egg hatchability reduced to 45-90%, depending on residual genome; dorsal appendages of chorion convoluted or fused (King and Koch, 1963, Quant. J. Microscop. Sci. 104: 297-320); adult emergence lowered to 33-85%. (Doane, 1963, DIS. 37: 73-74). Males viable and fertile. Heterozygotes show desiccation tolerance superior to that of wild type or adp60 homozygotes (Clark and Doane, 1983, Hereditas 99: 165-75). RK3. cytology: Placed in 55A-C1 based on its inclusion in Df(2R)PC4 = Df(2R)55A;55F but not Df(2R)P29 = Df(2R)55C1-2;56B1-2 (Doane and Dumapias, 1987, DIS 66: 49). # adpfs: adipose-female sterile origin: Spontaneous. discoverer: Counce, 1956. synonym: fs(2)adp: female sterile(2) adipose. references: Doane, 1959, Genetics 44: 506. 1960a, J. Exp. Zool. 145: 1-22 (fig.). 1960b, J. Exp. Zool. 145: 23-42. 1961, J. Exp. Zool. 146: 275-98. phenotype: Adult fat body phenotype like adp60; lipid accumu- lated at expense of glycogen in fat body; yolk deposition in ovaries retarded; carbohydrate levels low in 8-day-old adults (Cummings and Ganetzky, 1972, DIS 30: 48. Corpus allatum hypertrophies in mated females to same degree as in adp60. Females completely sterile; sterility autonomous. Eggs laid by homozygotes show meiotic or mitotic abnormalities, or both, never develop beyond early cleavage stages; chorion, chorionic filaments and vitelline membrane defective in some. Males 78% fertile. Heterozygotes fertile, but females become sterile with age. Viability generally good but longevity reduced; homozygotes with selective advantage under starvation; hetero- zygotes superior under desiccation. Average water content of well-fed adults reduced; percentage of lipids, as a function of dry body weight, almost double that of wild type. Iodine numbers show greater degree of saturation of mutant lipid extracts than of wild type. RK3. #*ae: aeroplane location: 2-55.8. origin: Spontaneous. discoverer: Mohr, 26k24. references: Quelprud, 1931, Hereditas 15: 97-119 (fig.). phenotype: Wings spread, balancers drooping. Overlaps wild type. RK3. #*Ae: Aechna location: 3- (rearrangement). origin: X ray induced. discoverer: Belgovsky, 45a14. references: 1946, DIS 20: 63. phenotype: Wings spread at right angles to body axis. Homozy- gous lethal. RK1A. other information: Reduced crossing over in the th-e region suggests presence of pericentric inversion. # aea: see dv2 # aeroplane: see ae # ag: agametic location: 1-20.7. origin: Spontaneous. references: Engstrom, Caulton, Underwood, and Mahowald, 1982, Dev. Biol. 91: 163-70 (fig.). phenotype: Maternal effect mutant; approximately 40% of gonads of progeny of homozygous females agametic. Although some eggs of homozygous females exhibit abnormal polar granules, normal numbers of pole cells form; some pole cells abnormal with degenerating polar granules and nuclear bodies, but pole cells reach gonads at 14 hr of development and then in 40% of the gonads become necrotic and disappear; responses of right and left gonads correlated. Phenotype most pronounced at 25, decreasing at higher and lower temperatures. Mutant not com- pletely recessive; expression in progeny of heterozygous females half that in those of homozygotes. cytology: Placed between 7B4 and 7C1 based on its position to the right of ct and its inclusion in Df(1)ct268-42 = Df(1)7A5-6;7B8-C1. #*agl: angle winglike location: 1- (not located). origin: Recovered among descendants of flies treated with natural gas. discoverer: Mickey, 49c7. synonym: Originally called angle wing but this name preoccupied by ang. references: 1950, DIS 24: 60. phenotype: Wing bent upward in middle. Overlaps wild type. RK3. # agn: agnostic location: 1-38.9. references: Savvateeva, Korochkina, Peresleny, and Kamyshev, 1985, DIS 61: 144. Savvateeva, Peresleny, Ivanushina, and Korochkin, 1985, Dev. Genet 5: 157-72. phenotype: Identified as three temperature sensitive lethal mutations. Adenylate cyclase activity somewhat higher than normal at 22 and readily activated at 29. Phosphodiesterase activity assayed in heat-pretreated homogenates higher than normal. Locomotor activity decreased and learning activity increased at 22, like dnc at 29. alleles: allele origin synonym ___________________________ agn1 EMS l(1)ts398 agn2 EMS l(1)ts622 agn3 EMS l(1)ts980 # agq: atrophie gonadique location: 2-3 polygenic. origin: Recovered from natural population on French Mediter- ranean coast. references: Periquet, 1970, DIS 45: 33. 1979, Biol. Cell. 33: 33-38. phenotype: Gonads atrophic either unilaterally or bilaterally owing to pole cell degeneration. Degree of effect correlated with both temperature during the first hours of development and with the number of agq-derived autosomes. Pole cells, but not oocytes, thermosensitive. Responses of right and left gonads correlated. Penetrance higher in females than males. # al: aristaless location: 2-0.4 [Golubovsky, Kulakov, and Korochkina, 1978, Genetika (Moscow) 14: 294-305]. references: Morgan, Bridges, and Sturtevant, 1925, Bibliog. Genet. 2: 213 (fig.). Stern and Bridges, 1926, Genetics 11: 510 (fig.). phenotype: Aristae strongly reduced. Postscutellars widely separated and erect but strongly divergent. Scutellum shor- tened; sternopleurals irregular in size, position, and number; wings slightly bowed downward, narrowed, and pointed; first longitudinal vein raised and thickened. Tarsal claws transformed into bristle-like structures or absent; effect enhanced by presence of th or ssa40a or both [Mglinetz and Ivanova, 1975, Genetika (Moscow) 11, 4: 88-96]. Enhances transformations of AntpNS [Mikuta and Mglinetz, 1978, Genetika (Moscow) 14: 1578-85] and ssa40a; al ssa40a flies exhibit partial transformation of third antennal segment to basi- tarsus; anomalous outgrowths of distal basitarsus and foreshortening of second and third tarsal joints of thoracic legs; spineless phenotype also enhanced. al females exhibit reduced mating success (Burnet, Connolly, and Dennis, 1971, Anim. Behav. 19: 409-15). RK1. alleles: allele origin discoverer ref ( comments ________________________________________________________________ al1 spont Bridges, 17k7 2, 6, 7 viable al2 spont Stern, 26a 7 al1; semilethal; female sterile al4 spont Bridges, 33l27 1, 2 al1; lethal; In(2LR)21C1-2;41C al36 X ray Glass, 36c 2, 3 =al1; viable *alM60 X ray Meyer, 60f 2, 5 lethal; In(2LR); variegated? alv X ray E.B. Lewis, 1940 1 lethal; In(2LR)21B-C1;41; variegated ( 1 = Bridges, 1935, DIS 3: 5; 2 = CP627; 3 = Glass, 1939, DIS 12: 47; 4 = Korochkina and Golubovsky, 1978, DIS 53: 197-200; 5 = Meyer, 1963, DIS 37: 50; 6 = Morgan, Bridges, and Sturtevant, 1925, Bibliog. Genet. 2: 213 (fig.); 7 = Stern and Bridges, 1926, Genetics 11: 510-511 (fig.). | Phenotype defined with respect to homozygous viablility and strength of expression in comparison with al1. cytology: Placed in 21C1-2 doublet on the basis of its inclu- sion in Df(2L)al = Df(2L)21B8-C1;21C8-D1 but not in Df(2L)S5 = Df(2L)21C2-3;22A3-4 (Lewis, 1945, Genetics 30: 137-166). # al8 phenotype: Homozygous lethal; 1% survival in combination with Df(2L)al = Df(2L)21B8-C1;21C8-D1; survivors have reduced aris- tae, broad thorax, arched wings with incomplete veins, enlarged eyes. cytology: Associated with In(2LR)al8 = In(2LR)21C1-2;41C. # al-b: see aa # ala: see dyala # ala parvae: see dyala # | alanyl dopamine hydrolase: see t # | alanyl dopamine synthetase: see e # alarless: see alr # alb: alberich location: 2-(unmapped). origin: Induced by ethyl methanesulfonate. references: Tearle and Nusslein-Volhard, 1987, DIS 66: 209-26. phenotype: Maternal-effect lethal; occasional embryo lacks abdominal segments (Lehmann). # Alcohol dehydrogenase: see Adh # ald: altered disjunction (A.T.C. Carpenter) location: 3-61. origin: Induced by ethyl methanesulfonate. references: O'Tousa, 1982, Genetics 102: 503-24. phenotype: Homozygous females display elevated levels of non- disjunction of X and fourth chromosomes (9.5 and 6.0% respec- tively); double exceptions are predominantly XX;0 and 0;44, products expected from nonhomologous disjunction; behavior of large autosomes nearly normal. Exchange frequencies normal, and sex-chromosome exchange tetrads contribute to exceptional products. # Ald: Aldolase location: 3-91.5. origin: Naturally occurring polymorphism. references: Voelker, Ohnishi, and Langley, 1979, Biochem. Genet. 17: 769-83. phenotype: Structural gene for fructose-biphosphate aldolase (EC 4.1.2.13). Enzyme multimeric based on the formation of heteromultimeric bands on gels from heterozygotes for electro- phoretic variants. Amino-acid sequence determined; protein is a 158-kd multimer comprising four 360-amino-acid polypeptides. Monomers show 71% identity with rabbit muscle aldolase (Malek, Suter, Frank, and Brenner-Holzach, 1985, Biochem. Biophys. Res. Comm. 126: 199-205). Mixed multimers of rabbit and Drosophila subunits able to function (Brenner-Holzach and Leu- thard, 1972, Eur. J. Biochem. 31: 423-26). Sequence analysis suggests alternating domains of alpha helix and beta sheet; domain boundaries correspond to boundaries between exons as seen in rat-liver aldolase (Sawyer, Fothergill-Gilmore, and Freemont, 1988, Biochem. J. 249: 789-93). cytology: Placed in 97A-B on the basis of its being between the autosomal breakpoints of T(Y;3)R87 = T(Y;3)97A and T(Y;3)B158 = T(Y;3)97B. alleles: Two electrophoretic variants described; Ald4 product migrates toward the anode more rapidly than that of Ald2. # Aldehyde oxidase: see Aldox # Aldolase: see Ald # Aldox-1: Aldehyde oxidase-1 location: 3-57.2 (between red and sbd). origin: Naturally occurring polymorphism. synonym: Ao. references: Dickinson, 1970, Genetics 66: 487-96. Warner, Watts, and Finnerty, 1980, Mol. Gen. Genet. 180: 449-53. Warner and Finnerty, 1981, Mol. Gen. Genet. 184: 92-96. Bogart and Bernini, 1981, Biochem. Genet. 19: 929-46. phenotype: Structural gene for aldehyde oxidase [AO-1 (EC 1.2.3.1)]. A molybdenum-containing homodimer with subun- its of 140,000-dalton molecular weight. As with other molybdenum hydroxylases, activity is inhibited by tungsten and depends on the presence of a low-molecular-weight cofactor (Warner and Finnerty). Enzyme activity increases nonuniformly during development with step increases at pupation and midway through pupal stage. First increase appears to be controlled by a closely linked cis-acting element (Dickinson, 1975, Dev. Biol. 42: 131-40) and the latter by Aldox-2+ (Bentley and Williamson, 1979, Z. Naturforsch. 34: 304-05). Control independent of that of lpo located 0.08 unit to the left (Dic- kinson and Weisbrod, 1976, Biochem. Genet. 14: 709-21). Enzyme activity absent in cin (Browder and Williamson, 1976, Develop. Biol. 53: 241-49) and mal and reduced in lxd (Cour- tright, 1967, Genetics 57: 25-39); cross-reacting material observed in all three genotypes (Browder, Wilkes, and Tucker, 1982, Biochem. Genet. 20: 111-24). These mutants presumably affect the availability of molybdenum cofactor (Warner and Finnerty). Autonomous in transplants. Enzyme composition in egg and early larva reflects maternal genotype, giving way to that of zygotic genotype during larval life. Tissue specifi- city varies with stage and strain (Dickinson, 1972, Genetics 71: s14; Cypher, Tedesco, Courtright and Kumaran, 1982, Biochem. Genet. 20: 315-32). Heptaldehyde serves as specific substrate (Cypher et al.). Differential staining for enzyme noted in different compartments of the wing imaginal disc (Kuhn and Cunningham, 1976, Genetics 83: s42). alleles: Three electrophoretic variants superscripted 1, 2, and 3 in order of increasing mobility described by Dickinson (1970) presumably correspond to Aldox-14, Aldox-16, and Aldox-18 (1978, DIS 53: 117); 6 electrophoretic variants num- bered in order of increasing mobility from 1 through 6 described by Langley, Tobari, and Kojima (1974, Genetics 78: 921-36). Correspondence of two sets of alleles unknown. Two null alleles superscripted n1 and n2 are homozygous viable but produce no recognizible product either in the form of enzyme activity or by the formation of heterodimers with func- tional gene products; however, cross-reacting material found in larval hemolymph but not in extracts of adults (Browder et al., 1982). Thirteen other null alleles isolated from natural populations in Great Britain (AldoxnGB1 to AldoxnGB4) and North Carolina (AldoxnNC1 to AldoxnNC9); all thirteen exhibit residual enzyme activity and except for AldoxnGB1 are Aldox4 derivatives and fail to participate in heterodimer formation with normal gene products. AldoxnGB1 is an Aldox8 derivative and forms heterodimers (Burkhart, Montgomery, Langley, and Voelker, 1984, Genetics 107: 295-306). lao: low aldehyde oxidase (Collins, Duck, and Glassman, 1971, Biochem. Genet. 5: 1-13) considered allelic based on its phenotype and genetic position (3-56); aldehyde oxidase levels of Aldoxn/Aldoxlao higher than expected if Aldoxn amorphic. cytology: Placed in region between 88F9 and 89B4 on the basis of its inclusion in Df(3)sbd105 = Df(3R)88F9-88A1;89B4-5 but not Df(3R)sbd45 = Df(3R)89B1-4;89B10-13 (Spillmann and Nothiger, 1978, DIS 53: 124). Narrowed to 89A1-2 by Langhout and van Breugel (1985, DIS 61: 181) on basis of reduced staining of that doublet in Aldoxn1. # Aldox-1Pa1 origin: Polymorphic in laboratory and natural populations. references: Dickinson, 1975, Dev. Biol. 42: 131-40. phenotype: Exhibits substantial increase in enzyme activity between late larval and early pupal stages followed by a second increase in late pupal stage. Results in relatively high pupal:adult activity ratio. # Aldox-1Pa2 origin: Polymorphic in laboratory and natural populations. references: Dickinson, 1975, Dev. Biol. 42: 131-40. phenotype: Exhibits little change in enzyme activity between late larval and early pupal stages, but there is a substantial increase in late pupal and adult stages. Results in rela- tively low pupal:adult activity ratio. Aldox-1Pa1/Aldox-1Pa2 has intermediate phenotype. other information: 1.5% recombination with electrophoretic Aldox-1 alleles recorded. The difference between Pa1 and Pa2 postulated to reside in a cis-acting site that exerts temporal control on gene activity. # Aldox-1Pb1 origin: Polymorphic in natural population from Lima, Peru. references: Dickinson, 1978, J. Exp. Zool. 206: 333-42. phenotype: Cytochemically, enzyme activity in paragonia uni- formly distributed and high at eclosion. By end of first week of adult life enzyme accumulated into intracellular bodies giving accessory gland a spotted appearance. alleles: Aldox-1Pb2 characterized by lower activity that remains uniformly distributed in paragonia as detected histo- chemically. other information: Not separated genetically from electro- phoretic alleles of Aldox-1. Pb1 and Pb2 postulated to differ in a cis-acting control site with tissue-specific effects on gene activity. # aldox2: aldehyde oxidase 2 location: 2-82.9 (based on 112 c-px recombinants). origin: Naturally occurring polymorphism. references: Bentley and Williamson, 1979, Z. Naturforsch. 34: 304-05. 1980, Genetics 94: s8. Meidinger and Bentley, 1986, Biochem. Genet. 24: 683-99. Bentley, Meidinger, and Braaten, 1989, Biochem. Genet. 27: 99-118. phenotype: Not a structural gene for aldehyde oxidase. Homozy- gotes for aldox2 fail to show increased levels of molybdoen- zymes, aldehyde oxidase, pyridoxal oxidase, sulfite oxidase, and xanthine oxidase, that normally occur late in the pupal period; adult levels lower than normal. Enzyme activity less sensitive to tungsten and more responsive to molybdenum than in wild type; aldehyde oxidase activity, at least, more heat labile and pH optimum slightly more acidic than normal (Meid- inger and Bentley, 1984, Genetics 107: s73). Duplication of aldox2+ without effect on enzyme levels. cytology: Placed in region 54 based on the failure of YP2D from T(Y;2)H149 = T(Y;2)h21;54F to cover it and its genetic map position to the right of Amy, which has been placed in 54A1-B1 by in situ hybridization. # ale: almond eye location: 3-47.5 (located with respect to D and Sb). origin: Spontaneous in natural population. references: Golubovsky and Zakharov, 1972, DIS 49: 112. Golubovsky, Ivanov, and Zakharov, 1973, Genetika (Moscow) 9(8): 168-71. phenotype: In homozygotes, eye almond shaped but with normal facet development. Phenotype normal in heterozygotes with normal third but mutant when heterozygous to D. Dfd/ale show normal eye size, and 20% of flies show tufted vibrissae characteristic of Dfd/+. ale Mc homozygotes completely eye- less. other information: Both Dfd and ale map to 47.5. No wild-type recombinants recovered among 569 tested progeny of Dfd/ale females. ale acts as a transdominant suppressor of Dfd. # Alin: Aliesterase-negative location: 3- (not located). origin: Spontaneous. synonym: ali: aliesteraseless. references: Ogita, 1961, Botyu-Kagaku 26: 93-97. 1962, DIS 36: 103. phenotype: Probably the structural gene for aliesterase [ALI (EC 3.1.1.1)]. Homozygotes for Alin practically unable to hydrolyze methyl butyrate, whereas wild type shows high activity; Alin/+ exhibits intermediate activity. Homozygotes shown by Beckman and Johnson to lack a normally present esterase that migrates slowly on starch gel (their band F). RK3. alleles: Alin is a null allele; no other variants reported. # Alkaline phosphatase: see Aph and Aph-2 # aliesteraseless: see Alin # almond: see Dfdr # almondex: see amx # almondex-55: see lzK # almond eye: see ale #*alo: alopecia location: 1-38.3. origin: Induced by 2-chloroethyl methanesulfonate. discoverer: Fahmy, 1956. references: 1958, DIS 32: 67. phenotype: Abdominal hairs much reduced in number; pigmentation frequently lighter and patchy. Effect very pronounced in females reared at 25 but overlaps wild type in both sexes when reared at a low temperature. Viability and fertility good in males but reduced in females. RK3. # Alp: Abnormal leg pattern location: 2-10. references: Tearle and Nusslein-Volhard, 1987, DIS 66: 209-26. phenotype: Defined by two dominant gain-of-function alleles. Heterozygotes viable with fusion of metatarsal and second tar- sal segments. Alp1/Alp2 is pupal lethal with more extreme tarsal fusions. alleles: Two X-ray induced alleles. Alp1 is associated with T(2;3)XT1 and Alp2 is associated with T(2;4)X2. cytology: Placed in 23F6-24A1 based on breakpoint common to translocations. # alpha: see tyr-1 # alpha methyldopa hypersensitive: see amd #*alr: alarless location: 3- (not located). origin: Spontaneous. discoverer: Steinberg, 40b. references: 1940, DIS 13: 51. phenotype: Outer postalar bristle always missing; posterior supra-alar missing in about 80% of the flies. Anterior scu- tellars, humerals, and notopleurals frequently duplicated. Never overlaps. Viability and fertility excellent. RK3. # ALS: see Acr96A # Altered abdomen: see Aa # altered disjunction: see ald # Alu: Alula location: 2-54.9 (Muller places Alu to the left of pr). origin: Spontaneous. discoverer: Bridges, 38a12. references: Curry, 1939, DIS 12: 45. phenotype: Heterozygote has alula fused to main wing; wings often bent, broader. May overlap wild type but intensified by cold and by heterozygous ds with buckling effect increased. Homozygote at 19 shows extreme buckling owing to rotation of wing and alula. Homozygote viable and resembles heterozygote. RK2. alleles: *Alu56c (CP627). #*alw: arclike wing location: 2- (near b). discoverer: Sturtevant, 1948. references: 1948, DIS 22: 55. phenotype: Wings evenly bent downward at tips. Overlaps wild type. RK2.