This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Greer, C Articles by Schekman, R Search for Related Content PubMed PubMed Citation Articles by Greer, C Articles by Schekman, R

Actin from Saccharomyces cerevisiae.

ABSTRACT

Inhibition of DNase I activity has been used as an assay to purify actin from Saccharomyces cerevisiae (yeast actin). The final fraction, obtained after a 300-fold purification, is approximately 97% pure as judged by sodium dodecyl sulfate-gel electrophoresis. Like rabbit skeletal muscle actin, yeast actin has a molecular weight of about 43,000, forms 7-nm-diameter filaments when polymerization is induced by KCl or Mg2+, and can be decorated with a proteolytic fragment of muscle myosin (heavy meromyosin). Although heavy meromyosin ATPase activity is stimulated by rabbit muscle and yeast actins to approximately the same Vmax (2 mmol of Pi per min per mumol of heavy meromyosin), half-maximal activation (Kapp) is obtained with 14 micro M muscle actin, but requires approximately 135 micro M yeast actin. This difference suggests a low affinity of yeast actin for muscle myosin. Yeast and muscle filamentous actin respond similarly to cytochalasin and phalloidin, although the drugs have no effect on S. cerevisiae cell growth.

This article has been cited by other articles:

• Takaine, M., Mabuchi, I. (2007). Properties of Actin from the Fission Yeast Schizosaccharomyces pombe and Interaction with Fission Yeast Profilin. J. Biol. Chem. 282: 21683-21694 [Abstract] [Full Text]  
• McKane, M., Wen, K.-K., Meyer, A., Rubenstein, P. A. (2006). Effect of the Substitution of Muscle Actin-specific Subdomain 1 and 2 Residues in Yeast Actin on Actin Function. J. Biol. Chem. 281: 29916-29928 [Abstract] [Full Text]  
• Trelles-Sticken, E., Adelfalk, C., Loidl, J., Scherthan, H. (2005). Meiotic telomere clustering requires actin for its formation and cohesin for its resolution. J. Cell Biol. 170: 213-223 [Abstract] [Full Text]  
• Wang, L., Merz, A. J., Collins, K. M., Wickner, W. (2003). Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion. J. Cell Biol. 160: 365-374 [Abstract] [Full Text]  
• Musib, R., Wang, G., Geng, L., Rubenstein, P. A. (2002). Effect of Polymerization on the Subdomain 3/4 Loop of Yeast Actin. J. Biol. Chem. 277: 22699-22709 [Abstract] [Full Text]