Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M509141200 on December 7, 2005

J. Biol. Chem., Vol. 281, Issue 8, 4949-4957, February 24, 2006
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
281/8/4949    most recent
M509141200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kambara, T.
Right arrow Articles by Ikebe, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kambara, T.
Right arrow Articles by Ikebe, M.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

A Unique ATP Hydrolysis Mechanism of Single-headed Processive Myosin, Myosin IX*

Taketoshi Kambara and Mitsuo Ikebe1

From the Department of Physiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655

Recent studies have revealed that myosin IX is a single-headed processive myosin, yet it is unclear how myosin IX can achieve the processive movement. Here we studied the mechanism of ATP hydrolysis cycle of actomyosin IXb. We found that myosin IXb has a rate-limiting ATP hydrolysis step unlike other known myosins, thus populating the prehydrolysis intermediate (M·ATP). M·ATP has a high affinity for actin, and, unlike other myosins, the dissociation of M·ATP from actin was extremely slow, thus preventing myosin from dissociating away from actin. The ADP dissociation step was 10-fold faster than the overall ATP hydrolysis cycle rate and thus not rate-limiting. We propose the following model for single-headed processive myosin. Upon the formation of the M·ATP intermediate, the tight binding of actomyosin IX at the interface is weakened. However, the head is kept in close proximity to actin due to the tethering role of loop 2/large unique insertion of myosin IX. There is enough freedom for the myosin head to find the next location of the binding site along with the actin filament before complete dissociation from the filament. After ATP hydrolysis, Pi is quickly released to form a strong actin binding form, and a power stroke takes place.


Received for publication, August 18, 2005 , and in revised form, December 2, 2005.

* This work was supported by National Institute of Health Grants AR 048526, AR 048898, and AR 41653. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 To whom correspondence should be addressed: Dept. of Physiology, University of Massachusetts Medical School, 55 Lake Ave. N., Worcester, MA 01655. Tel.: 508-856-6698; Fax: 508-856-4997; E-mail: mitsuo.ikebe{at}umassmed.edu.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
S. Struchholz, K. Elfrink, U. Pieper, G. Kalhammer, U. Honnert, A. Grutzner, W. A. Linke, W. Liao, and M. Bahler
Functional Role of the Extended Loop 2 in the Myosin 9b Head for Binding F-actin
J. Biol. Chem., February 6, 2009; 284(6): 3663 - 3671.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
F. van den Boom, H. Dussmann, K. Uhlenbrock, M. Abouhamed, and M. Bahler
The Myosin IXb Motor Activity Targets the Myosin IXb RhoGAP Domain as Cargo to Sites of Actin Polymerization
Mol. Biol. Cell, April 1, 2007; 18(4): 1507 - 1518.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. C. Krzysiak and S. P. Gilbert
Dimeric Eg5 Maintains Processivity through Alternating-site Catalysis with Rate-limiting ATP Hydrolysis
J. Biol. Chem., December 22, 2006; 281(51): 39444 - 39454.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Kambara, S. Komaba, and M. Ikebe
Human Myosin III Is a Motor Having an Extremely High Affinity for Actin
J. Biol. Chem., December 8, 2006; 281(49): 37291 - 37301.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement