Distribution and genetic basis of arginine kinase in wild type and flightless mutants ofDrosophila melanogaster
✍ Scribed by James, Judith M. ;Collier, Glen E.
- Publisher
- John Wiley and Sons
- Year
- 1988
- Tongue
- English
- Weight
- 689 KB
- Volume
- 248
- Category
- Article
- ISSN
- 0022-104X
No coin nor oath required. For personal study only.
✦ Synopsis
Arginine kinase (AK) activity in Drosophila melanogaster has been localized to specific tissues, traced through developmental stages, and inferred to be the product of a single gene. AK is most abundant in muscle, particularly in larval and adult body-wall muscle and digestive tract, and in adult indirect flight muscle (IF'M) and legs. Low but detectable levels are present in larval imaginal discs, brain, salivary glands, and adult head and reproductive tract. Electrophoretic analyses of a series of developmental stages, as well as prepupal and adult tissues, show only one cytoplasmic isozyme. Since an allozymic variant has the same altered electrophoretic mobility in all stages and tissues, a single structural gene is inferred for AK. A variety of flightless mutants were compared to wild type in regard to AK activity and distribution.
MATERIALS AND METHODS
Sources
of fly stocks distribution (Eppenberger et al., '83; Walliman et Sources for mutants were as follows: Ifm(2)-and al., 'SS), myofibrillar association (Turner et al., ,731, Ifm(3)-from K. Mogami (Univ. of Tokyo); grounded developmental profile (Eppenberger et al., ,641, and ( 9nd2), heldup (hdp4), and upheld (up") from T. Hogenetic basis are well documented (Roberts and myk, Univ. of Virginia; raised (rsd from J. Mahaf-Grace, '80; Rosenberg et al., '81). Recently, the fey, Indiana Univ.; flapwing (f2w) from E. Gese, structural gene for this enzyme has been isolated Cal. Inst. Tech. Stuck-up (Stp) (Collier and Finke, and sequenced from several vertebrate species (e.g., '84), Outstretched (Os), and Curloid (CuO were iso- Buskin et al., '85). lated in our laboratory. A rare allozymic variant of Arginine kinase (EC 2.7.3.3) is the phosphagen AK, exhibiting slower electrophoretic mobility kinase of arthropods (Blethan and Kaplan, '68; (designated A r g p ) , was isolated from a natural Morrison, '73) but is less well known. The tissue distribution of the cytoplasmic form has been reported for only a few arthropods (Blethan and Kapand Eppenberger, '73). None of these studies was Z O O ~O ~Y ,