Heat shock gene activation by mutant actin is independent of myofibril degeneration in Drosophila muscle

Artificially mutagenized Drosophila Act88F actin genes with triple and double mutations were expressed in the indirect flight muscles of transgenic flies. The triple mutant actin, GD246T (Gly-36→Glu, Glu-83→Asp, and Gly-246→Asp), induced heat shock protein (hsp) synthesis without affecting flight ab...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1991-05, Vol.109 (5), p.670-673
Main Authors: Sakai, Y, Okamoto, H, Mogami, K, Matsuo, H, Hotta, Y
Format: Article
Language:English
Subjects:
actin
Actins - genetics
Animals
Drosophila
Drosophila - genetics
flight muscles
Gene Expression Regulation
genes
genetically modified organisms
heat shock proteins
Heat-Shock Proteins - genetics
muscles
Muscles - metabolism
Muscles - pathology
Mutation
Myofibrils - pathology
Phenotype
Transcriptional Activation
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Summary:Artificially mutagenized Drosophila Act88F actin genes with triple and double mutations were expressed in the indirect flight muscles of transgenic flies. The triple mutant actin, GD246T (Gly-36→Glu, Glu-83→Asp, and Gly-246→Asp), induced heat shock protein (hsp) synthesis without affecting flight ability. On the other hand, the double mutation, GD245D (Gly-36→Glu and Glu-83→Asp), disrupted myofibrils but induced little hsp synthesis. These results demonstrate that myofibril degeneration is not the primary cause of the anomalous heat shock gene activation by mutant actins.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a123438