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PMID: 1534298 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Site-specific amino-terminal mutants of yeast-expressed beta-actin. Characterization of the interaction with myosin and tropomyosin.

FEBS letters ·Vol. 303 ·No. 1 ·1992-05-25 ·Pages 59-63

Aspenström P, Lindberg U, Karlsson R

Abstract

Neutral or charge-shifting mutagenesis of beta-actin at positions 3 and 4 strongly influenced the actomyosin interaction under non-rigor conditions. The polymerization behaviour and tropomyosin binding properties on the other hand remained unaffected.

MeSH Terms

Actins/genetics,metabolism Adenosine Triphosphatases/metabolism Chromatography, Liquid Electrophoresis, Polyacrylamide Gel Genes, Fungal Mutagenesis, Site-Directed Myosins/metabolism Saccharomyces cerevisiae/genetics Tropomyosin/metabolism

Chemicals

Actins Tropomyosin Adenosine Triphosphatases Myosins

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Aspenström P

Dept. Developmental Biology, Uppsala University, Sweden.

Lindberg U

Karlsson R

Article Info

Journal

FEBS letters

Abbr.

FEBS Lett

ISSN

0014-5793

DOI

10.1016/0014-5793(92)80477-x

Published

1992-05-25

Pages

59-63

Language

English

Region

England

NLM ID

0155157

Subset

Corrections

ErratumIn

External Links

PubMed source DOI: 10.1016/0014-5793(92)80477-x View journal details

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Site-specific amino-terminal mutants of yeast-expressed beta-actin. Characterization of the interaction with myosin and tropomyosin.

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