Actin mutations that show suppression with fimbrin mutations identify a likely fimbrin-binding site on actin

doi:10.1083/jcb.126.2.413

This Article

	Full Text (PDF, 2845K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Honts, J. E.
	Articles by Adams, A. E.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Honts, J. E.
	Articles by Adams, A. E.


Social Bookmarking

	What's this?

ARTICLES

Actin mutations that show suppression with fimbrin mutations identify a likely fimbrin-binding site on actin

JE Honts, TS Sandrock, SM Brower, JL O'Dell and AE Adams
Department of Molecular and Cellular Biology, University of Arizona, Tucson 85721.

Actin interacts with a large number of different proteins that modulate its assembly and mediate its functions. One such protein is the yeast actin-binding protein Sac6p, which is homologous to vertebrate fimbrin (Adams, A. E. M., D. Botstein, and D. G. Drubin. 1991. Nature (Lond.). 354:404-408.). Sac6p was originally identified both genetically (Adams, A. E. M., and D. Botstein. 1989. Genetics. 121:675-683.) by dominant, reciprocal suppression of a temperature-sensitive yeast actin mutation (act1-1), as well as biochemically (Drubin, D. G., K. G. Miller, and D. Botstein. 1988. J. Cell Biol. 107: 2551-2561.). To identify the region on actin that interacts with Sac6p, we have analyzed eight different act1 mutations that show suppression with sac6 mutant alleles, and have asked whether (a) these mutations occur in a small defined region on the crystal structure of actin; and (b) the mutant actins are defective in their interaction with Sac6p in vitro. Sequence analysis indicates that all of these mutations change residues that cluster in the small domain of the actin crystal structure, suggesting that this region is an important part of the Sac6p-binding domain. Biochemical analysis reveals defects in the ability of several of the mutant actins to bind Sac6p, and a reduction in Sac6p-induced cross-linking of mutant actin filaments. Together, these observations identify a likely site of interaction of fimbrin on actin.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Pittman, Y. R., Kandl, K., Lewis, M., Valente, L., Kinzy, T. G. (2009). Coordination of Eukaryotic Translation Elongation Factor 1A (eEF1A) Function in Actin Organization and Translation Elongation by the Guanine Nucleotide Exchange Factor eEF1B{alpha}. J. Biol. Chem. 284: 4739-4747 [Abstract] [Full Text]
Gheorghe, D. M., Aghamohammadzadeh, S., Rooij, I. I. S.-d., Allwood, E. G., Winder, S. J., Ayscough, K. R. (2008). Interactions between the Yeast SM22 Homologue Scp1 and Actin Demonstrate the Importance of Actin Bundling in Endocytosis. J. Biol. Chem. 283: 15037-15046 [Abstract] [Full Text]
Galkin, V. E., Orlova, A., Cherepanova, O., Lebart, M.-C., Egelman, E. H. (2008). High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex. Proc. Natl. Acad. Sci. USA 105: 1494-1498 [Abstract] [Full Text]
Moseley, J. B., Goode, B. L. (2006). The Yeast Actin Cytoskeleton: from Cellular Function to Biochemical Mechanism. Microbiol. Mol. Biol. Rev. 70: 605-645 [Abstract] [Full Text]
Bennett, V., Baines, A. J. (2001). Spectrin and Ankyrin-Based Pathways: Metazoan Inventions for Integrating Cells Into Tissues. Physiol. Rev. 81: 1353-1392 [Abstract] [Full Text]
Volkmann, N., DeRosier, D., Matsudaira, P., Hanein, D. (2001). An Atomic Model of Actin Filaments Cross-Linked by Fimbrin and Its Implications for Bundle Assembly and Function. JCB 153: 947-956 [Abstract] [Full Text]
Munshi, R., Kandl, K. A., Carr-Schmid, A., Whitacre, J. L., Adams, A. E. M., Kinzy, T. G. (2001). Overexpression of Translation Elongation Factor 1A Affects the Organization and Function of the Actin Cytoskeleton in Yeast. Genetics 157: 1425-1436 [Abstract] [Full Text]
Asleson, C. M., Bensen, E. S., Gale, C. A., Melms, A.-S., Kurischko, C., Berman, J. (2001). Candida albicans INT1-Induced Filamentation in Saccharomyces cerevisiae Depends on Sla2p. Mol. Cell. Biol. 21: 1272-1284 [Abstract] [Full Text]
Whitacre, J. L., Davis, D. A., Toenjes, K. A., Brower, S. M., Adams, A. E. M. (2001). Generation of an Isogenic Collection of Yeast Actin Mutants and Identification of Three Interrelated Phenotypes. Genetics 157: 533-543 [Abstract] [Full Text]
Cheng, D., Marner, J., Rubenstein, P. A. (1999). Interaction in Vivo and in Vitro between the Yeast Fimbrin, SAC6P, and a Polymerization-defective Yeast Actin (V266G and L267G). J. Biol. Chem. 274: 35873-35880 [Abstract] [Full Text]
Sandrock, T. M., Brower, S. M., Toenjes, K. A., Adams, A. E. M. (1999). Suppressor Analysis of Fimbrin (Sac6p) Overexpression in Yeast. Genetics 151: 1287-1297 [Abstract] [Full Text]
Belmont, L., Patterson, G., Drubin, D. (1999). New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites. J. Cell Sci. 112: 1325-1336 [Abstract]
Cali, B. M., Doyle, T. C., Botstein, D., Fink, G. R. (1998). Multiple Functions for Actin during Filamentous Growth of Saccharomyces cerevisiae. Mol. Biol. Cell 9: 1873-1889 [Abstract] [Full Text]
Hanein, D., Matsudaira, P., DeRosier, D. J. (1997). Evidence for a Conformational Change in Actin Induced by Fimbrin (N375) Binding. JCB 139: 387-396 [Abstract] [Full Text]
Buchberger, A., Theyssen, H., Schr�der, H., McCarty, J. S., Virgallita, G., Milkereit, P., Reinstein, J., Bukau, B. (1995). Nucleotide-induced Conformational Changes in the ATPase and Substrate Binding Domains of the DnaK Chaperone Provide Evidence for Interdomain Communication. J. Biol. Chem. 270: 16903-16910 [Abstract] [Full Text]