Tetrahymena Elongation Factor-1α Binds to Hsp70 Family Proteins
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概要
- 論文の詳細を見る
Translation elongation factor 1α (EF-1α) catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosome. We previously reported that Tetrahymena EF-1α induced bundles of rabbit skeletalmuscle F-actin as well as Tetrahymena F-actin (Kurasawa et al., (1996) Zool. Sci. 13: 371–375), andthat Ca2+/calmodulin (CaM) regulated the F-actin-bundling activity of EF-1α without inhibition of the bindingbetween EF-1α and F-actin (Kurasawa et al.,(1996) J. Biochem. 119: 791–798). In this study, we investigatedEF-1α-binding proteins in Tetrahymena using a Tetrahymena EF-1α affinity column. TetrahymenaEF-1α bound directly to 74 kDa, 77 kDa, and 78 kDa proteins, in addition to CaM. The bindings of 74 kDa, 77kDa, and 78 kDa proteins to Tetrahymena EF-1α were Ca2+-independent and ATP-sensitive. The N-terminalamino acid sequence of the 74 kDa protein was similar to those of 70 kDa heat shock protein (hsp70) family.
- 社団法人日本動物学会の論文
- 1999-04-15
著者
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Numata Osamu
Graduate School of Life and Environmental Sciences, University of Tsukuba
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Numata Osamu
Institute of Biological Sciences University of Tsukuba
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Numata O
Graduate School Of Life And Environmental Sciences University Of Tsukuba
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Numata Osamu
Institute Of Biological Sciences Tsukuba University
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Watanabe Y
Jobu University
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KURASAWA Yasuhiro
Institute of Biological Sciences,University of Tsukuba
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WATANABE Yoshio
Jobu University
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Watanabe Y
Tokyo Inst. Technol. Yokohama
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Kurasawa Yasuhiro
Institute Of Biological Sciences University Of Tsukuba
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