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PMID: 2762312 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Coupling of nonpolymerizable monomeric actin to the F-actin binding region of the myosin head.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 86 ·No. 16 ·1989-08-00 ·Pages 6028-32

Bettache N, Bertrand R, Kassab R

Abstract

Polymerizations of skeletal G-actin induced by salt and myosin subfragment 1 (S-1) were suppressed by reaction of G-actin with m-maleimidobenzoyl-N-hydroxysuccinimide ester. The G-actin derivative, containing few intramolecular crosslinks and a free maleimide group, was covalently coupled in solution to the S-1 heavy chain. The resulting complex could no longer bind to F-actin. The SH-1 and SH-2 thiols of S-1 were not involved in the complexation and the covalent link was shown to be exclusively on the 50-kDa segment of the S-1 heavy chain. The specific conjugation of the two proteins followed formation of a reversibly associated pyrophosphate-sensitive binary complex which was characterized by different approaches. Potentially, these complexes may be useful in developing the crystallography of actin-bound S-1.

MeSH Terms
Actins/metabolism Animals Electrophoresis, Polyacrylamide Gel Kinetics Molecular Weight Muscles/metabolism Myosins/metabolism Peptide Fragments/analysis Protein Binding Rabbits Trypsin
Chemicals
Actins Peptide Fragments Trypsin Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bettache N
Centre de Recherches de Biochimie Macromoléculaire du Centre National de la Recherche Scientifique, Unviersité de Montpellier, France.
Bertrand R
Kassab R
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.86.16.6028
Published
1989-08-00
Pages
6028-32
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC297768
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.86.16.6028 PMC Full Text View journal details
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