J. Biochem, 1996, Vol. 119, No. 4 791-798
© 1996 Japanese Biochemical Society
research-article |
F-Actin Bundling Activity of Tetrahymena Elongation Factor l
Is Regulated by Ca2+/Calmodulin1
*Institute of Biological Sciences, University of Tsukuba Tsukuba, Ibaraki 305
Joubu University Isesaki, Gumma 372
2To whom correspondence should be addressed. Tel: +81-298-53-6648, Fax: +81-298-53-6648 or 6614, E-mail: numata{at}sakura.ee.tsukuba.ac.jp
Translation elongation factor la (EF-la) catalyzes the GTP-dependent binding of amino-acyl-tRNA to the ribosome.Previously, Tetrahymena 14-nm filament-associated protein was identified as EF-la [Kurasawa et aL (1992) Exp. Cell Res; 203, 261–268]. This and several other studies suggest that EF-la functions not only in translation but also in regulation of some part of the cytoskeleton. Tetrahymena EF-l
bound to F-actin and induced bundling of F-actin. We investigated the effects of GTP/GDP and Ca2+calmodulin on F-actin bundling activity of EF-l. The presence of GTP, GDP, or guanylyl-imidodi-phosphate (GMP-PNP) slightly decreased the amount of EF-lbound to F-actin, but each had virtually no effect on the F-actin bundling activity. The formation of F-actin bundles by EF-l was Ca2+-insensitive. In the absence of Ca2+, calmodulin did not bind to EF-l and F-actin. On the other hand, in the presence of Ca2+, calmodulin directly bound to EF-l but did not have any serious influence on EF-l/F-actin binding. Under the conditions, electron microscopy demonstrated that Ca2+/calmodulin completely inhibited the F-actin bundling by EF-l. These results indicate that Ca2+/calmodulin regulates the F-actin bundling activity of EF-l without inhibition of the binding between EF-l and F-actin.
1 This work was supported by Research Fellowships of the Japan Society for the Promotion of Science for Young Scientists.
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