Myosin VIIB from Drosophila is a high duty ratio motor

doi:10.1074/jbc.M506765200

HOME

QUICK SEARCH:

	Author:		Keyword(s):
Year:		Vol:		Page:

A more recent version of this article appeared on September 16, 2005

This Article

	Full Text (Accepted Manuscript)
	All Versions of this Article: 280/37/32061 most recent M506765200v1
	Alert me when this article is cited
	Alert me if a correction is posted

Services

	Email this article to a friend
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new issues of the journal
	Download to citation manager
	Request Permissions

Citing Articles

	Citing Articles via HighWire
	Citing Articles via Google Scholar

Google Scholar

	Articles by Yang, Y.
	Articles by Sellers, J. R.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Yang, Y.
	Articles by Sellers, J. R.

Social Bookmarking

	What's this?

Papers In Press, published online ahead of print July 29, 2005
J. Biol. Chem, 10.1074/jbc.M506765200
Submitted on June 21, 2005
Revised on July 22, 2005
Accepted on July 29, 2005

Myosin VIIB from Drosophila is a high duty ratio motor

Yi Yang, Mihaly Kovacs, Elizabeth Xu, John B. Anderson, and James R. Sellers

Laboratory of Molecular Physiology, National Heart, Lung and Blood Institute, Bethesda, MD 20892-1762

Corresponding Author: sellersj{at}nhlbi.nih.gov

Myosin VII is an unconventional myosin widely expressed in organisms ranging from amoebae to mammals that has been shown to play vital roles in cell adhesion and phagocytosis. Here we present the first study of the mechanism of action of a myosin VII isoform. We have expressed a truncated single-headed Drosophila myosin VIIB construct in the baculovirus-Sf9 system that bound calmodulin light chains. Using steady-state and transient kinetic methods, we show that myosin VIIB exhibits a fast release of phosphate and a slower, rate-limiting ADP release from actomyosin. As a result, myosin VIIB will be predominantly strongly bound to actin during steady-state ATP hydrolysis (its duty ratio will be at least 80 %). This kinetic pattern is in many respects similar to that of the single-molecule vesicle transporters myosin V and VI. The enzymatic properties of myosin VIIB provide a kinetic basis for processivity upon possible dimerization via the C-terminal domains of the heavy chain. Our experiments also reveal conformational heterogeneity of the acto-myosin VIIB complex in the absence of nucleotide.

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:

Y. Takagi, Y. Yang, I. Fujiwara, D. Jacobs, R. E. Cheney, J. R. Sellers, and M. Kovacs
Human Myosin Vc Is a Low Duty Ratio, Nonprocessive Molecular Motor
J. Biol. Chem., March 28, 2008; 283(13): 8527 - 8537.
[Abstract] [Full Text] [PDF]

K. Ito, M. Ikebe, T. Kashiyama, T. Mogami, T. Kon, and K. Yamamoto
Kinetic Mechanism of the Fastest Motor Protein, Chara Myosin
J. Biol. Chem., July 6, 2007; 282(27): 19534 - 19545.
[Abstract] [Full Text] [PDF]

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]

Y. Yang, M. Kovacs, T. Sakamoto, F. Zhang, D. P. Kiehart, and J. R. Sellers
Dimerized Drosophila myosin VIIa: A processive motor
PNAS, April 11, 2006; 103(15): 5746 - 5751.
[Abstract] [Full Text] [PDF]

S. Watanabe, R. Ikebe, and M. Ikebe
Drosophila Myosin VIIA Is a High Duty Ratio Motor with a Unique Kinetic Mechanism
J. Biol. Chem., March 17, 2006; 281(11): 7151 - 7160.
[Abstract] [Full Text] [PDF]

A. Henn and E. M. De La Cruz
Vertebrate Myosin VIIb Is a High Duty Ratio Motor Adapted for Generating and Maintaining Tension
J. Biol. Chem., November 25, 2005; 280(47): 39665 - 39676.
[Abstract] [Full Text] [PDF]