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Molecular characterization of mutant actin genes which induce heat‐shock proteins in Drosophila flight muscles
Author(s) -
Okamoto Hitoshi,
Hiromi Yasushi,
Ishikawa Etsuko,
Yamada Takuma,
Isoda Kazuyoshi,
Maekawa Hideaki,
Hotta Yoshiki
Publication year - 1986
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1986.tb04251.x
Subject(s) - library science , biology , computer science
Heat‐shock proteins (hsps) are constitutively induced by the mutant actins in the Drosophila indirect flight muscles (IFM). We compared primary structures of the mutant actin genes (KM75 and HH5) which induce hsps and of the non‐inducing alleles (KM129 and KM88). The KM75 actin has lost 20 amino acids at the C‐terminus. The HH5 actin has only one amino acid substitution, from Gly‐336 to Ser. In KM129, the C‐terminal part of actin is replaced by novel amino acids. KM88 is a null allele, with an amber mutation early in the coding region of the mutated actin gene. Although all of the KM75, HH5 and KM129 actins have defects near the C‐terminus, only hsp‐inducing mutant actins cause enlargement of the IFM nuclei as well as a disruption of myofibrils even in the presence of two copies of the normal genes. We further consider the underlying mechanisms linking these features of the hsp‐inducing alleles.