Purification, characterization, and immimofluorescence localization of Saccharomyces cerevisiae capping protein

James F. Amatruda, John A. Cooper

Research output: Contribution to journalArticlepeer-review

93 Scopus citations

Abstract

Capping protein binds the barbed ends of actin filaments and nucleates actin filament assembly in vitro. We purified capping protein from Saccharomyces cervisiae. One of the two subunits is the product of the CAP2 gene, which we previously identified as the gene encoding the β subunit of capping protein based on its sequence similarity to capping protein β subunits in chicken and Dictyostelium (Amatruda, J. F., J. F. Cannon, K. Tatchell, C. Hug, and J. A. Cooper. 1990. Nature (Lond.). 344:352-354). Yeast capping protein has activity in critical concentration and low-shear viscometry assays consistent with barbedend capping activity. Like chicken capping protein, yeast capping protein is inhibited by PIP2. By immunofluorescence microscopy yeast capping protein colocalizes with cortical actin spots at the site of bud emergence and at the tips of growing buds and shmoos. In contrast, capping protein does not colocalize with actin cables or with actin rings at the site of cytokinesis.

Original languageEnglish (US)
Pages (from-to)1067-1076
Number of pages10
JournalJournal of Cell Biology
Volume117
Issue number5
DOIs
StatePublished - Jun 1992

ASJC Scopus subject areas

  • Cell Biology

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