Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by KATOH, T.
Right arrow Articles by MORITA, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by KATOH, T.
Right arrow Articles by MORITA, F.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1984, Vol. 96, No. 4 1223-1230
© 1984 Japanese Biochemical Society

research-article

Interaction between Myosin and F-Actin. Correlation with Actin-Binding Sites on Subfragment-11

Tsuyoshi KATOH and Fumi MORITA

Department of Chemistry, Faculty of Science, Hokkaido University Kita-ku, Sapporo, Hokkaido 060

F-Actin bindings to subfragment-1 (S-1) and S-1 after limited proteolysis by trypsin (S-1t) were studied in the absence and presence of ATP by means of ultracentrifugation. No significant difference in the affinities for F-actin was observed between S-1 and S-1t in the absence of ATP. In contrast, the affinity for F-actin in the presence of ATP was decreased about 50 times by the limited proteolysis of the S-1 heavy chain. The S-1 whose SH1 and SH2 groups were cross-linked by N,N'-p-phenylenedimaleimide bound F-actin weakly. The affinity for F-actin was similar to that of unmodified S-1 in the presence of ATP and was also decreased markedly by limited proteolysis of the cross-linked S-1. Reciprocals of the dissociation constant of acto-S-1 complex decreased markedly with increase of ionic strength in the presence of ATP, but decreased only slightly at the rigor state. All these results are consistent with our proposal that S-1 has two different actin binding sites, as reported previously (Katoh, T., Imae, S., & Morita, F. (1984) J. Biochem, 95, 447–454). The mechanism of activation of S-1 ATPase by F-actin is discussed.

1This study was supported in part by Grants-in-Aid from the Muscular Dystrophy Association of America, Inc., and from the Ministry of Education, Science and Culture of Japan.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
W.-L. Lee, E. M. Ostap, H. G. Zot, and T. D. Pollard
Organization and Ligand Binding Properties of the Tail of Acanthamoeba Myosin-IA. IDENTIFICATION OF AN ACTIN-BINDING SITE IN THE BASIC (TAIL HOMOLOGY-1) DOMAIN
J. Biol. Chem., December 3, 1999; 274(49): 35159 - 35171.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.