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Originally published In Press as doi:10.1074/jbc.M009561200 on November 28, 2000

J. Biol. Chem., Vol. 276, Issue 9, 6306-6312, March 2, 2001
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UNC-87 Is an Actin-bundling Protein*

Wolfgang J. Kranewitter, Jari YlanneDagger , and Mario Gimona§

From the Department of Cell Biology, Institute of Molecular Biology, Austrian Academy of Sciences, Billrothstrasse 11, A-5020 Salzburg, Austria and the Dagger  European Molecular Biology Laboratory, Department of Structural Biology, Mayerhofstrasse 1, D-69012 Heidelberg, Germany

The Caenorhabditis elegans unc-87 gene product is essential for the maintenance of the nematode body wall muscle where it is found colocalized with actin in the I band. The molecular domain structure of the protein reveals similarity to the C-terminal repeat region of the smooth muscle actin-binding protein calponin. In this study we investigated the in vitro function of UNC-87 using both the full-length recombinant molecule and several truncated mutants. According to analytical ultracentrifugation UNC-87 occurs as a monomer in solution. UNC-87 cosedimented with both smooth and skeletal muscle F-actin, but not with monomeric G-actin, and exhibited potent actin filament bundling activity. Actin binding was independent of the presence of tropomyosin and the actin cross-linking proteins filamin and alpha -actinin. Consistent with its actin bundling activity in vitro, UNC-87 tagged with green fluorescent protein associated with and promoted the formation of actin stress fiber bundles in living cells. These data identify UNC-87 as an actin-bundling protein and highlight the calponin-like repeats as a novel actin-binding module.

* This work was supported in part by grants from the Austrian Science Foundation (Fonds zur Förderung der wissenschaftlichen Forschung).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed. Tel.: 43-662- 63961-19; Fax: 43-662-63961-40; E-mail: mgimona@server1.imolbio. oeaw.ac.at

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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