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Zoolog Sci. 1996 Jun;13(3):371-5.

Characterization of F-actin bundling activity of Tetrahymena elongation factor 1 alpha investigated with rabbit skeletal muscle actin.

Author information

1
Institute of Biological Sciences, University of Tsukuba, Ibaraki, Japan.

Abstract

Elongation factor 1 alpha (EF-1 alpha) is an essential factor for protein synthesis in eukaryotes. Here, we demonstrated that Tetrahymena EF-1 alpha induced bundles of rabbit skeletal muscle F-actin as well as Tetrahymena F-actin in vitro, although Tetrahymena and skeletal muscle actins are different in some parts of their primary structures and in the binding abilities to some actin-binding proteins. Co-sedimentation experiments showed that the binding ratio of Tetrahymena EF-1 alpha to skeletal muscle F-actin in the bundles was 1 : 1. Electron microscopic observation showed that alkaline pH or high ionic strength reduced the bundling activity of Tetrahymena EF-1 alpha to some extent, although the EF-1 alpha seemed to be able to induce bundling of the F-actin within the range of physiological condition.

PMID:
9019273
DOI:
10.2108/zsj.13.371
[Indexed for MEDLINE]

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