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KMID : 0578319930030040433
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Molecules and Cells
1993 Volume.3 No. 4 p.433 ~ p.443
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Characterization of Drosophila melanogaster Act 88F Actin Allele with Point Mutation in Myosin Binding Site
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An, Hye-Suck
Mogami, Kaname/Yoo, Mi-Ae/Lee, Won-Ho
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Abstract
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We have characterized a mutation of the indirect flight muscle (IFM)-specific act88F actin gene of Drosophila melanogaster. Defective alleles were obtained from Drosophila third chromosomal dominant flightless mutants isolated (An, 1992). From the direct sequencing by the asymmetric polymerase chain reaction (PCR) amplification of the DNA fragments including the act88F gene coding region, we found that one actin mutation, designated as R95C, had their alteration site in arginine 95. In R95C mutation a single G-C to A-T transition converted arginine 95 to cystein in all the actin encoded in the IFM. According to the actin crystal structure and the studies through NMR and chemical cross linking, this site is considered to belong to the central region with myosin SI (Moir and Levine, 1986; Bertrand et al., 1988; Kabsch et al., 1990). Detailed analysis of R95C mutants shows that the actin encoded by the mutated gene is "antimorphic, that is, individuals having two normal and one mutant act88F genes still show the mutant phenotype. Mutant allele effectively destructs myofibrillar structure. And weak heat shock proteins (hsps) synthesis is induced in IFMs of R95C act88F mutant. Surprisingly we also found that R95C mutation caused marked disruption in the morphology of IFM fibers.
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