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Journal of Biochemistry Advance Access originally published online on September 10, 2007
Journal of Biochemistry 2007 142(4):481-490; doi:10.1093/jb/mvm161
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© 2007 The Japanese Biochemical Society.

Characterization of Native Myosin VI Isolated from Sea Urchin Eggs

Souhei Sakata1, Yuuko Watanabe1, Jiro Usukura2 and Issei Mabuchi1,*

1Division of Biology, Department of Life Sciences, Graduate School of Arts and Science, University of Tokyo, Komaba, Meguro-ku, Tokyo 153-8902; and 2Center for Cooperative Research in Advanced Science and Technology, Nagoya University, Nagoya, 464-0814, Japan

*To whom correspondence should be addressed. Department of Chemistry, Gakushuin University, 1-5-1 Mejiro, Toshima-ku, Tokyo 171-8588. Tel: +81-3-3986-0221, ext. 6421, Fax: +81-3-5992-1029, E-mail: issei.mabuchi{at}gakushuin.ac.jp

Received May 30, 2007; Accepted July 16, 2007


  Abstract

Myosin VI is a molecular motor that is ubiquitously expressed among eukaryotic cells, and thought to be involved in membrane trafficking and anchoring the organelle to actin cytoskeleton. Studies on myosin VI have been carried out using recombinant proteins, but native myosin VI has not been purified yet. Here we purified native myosin VI from sea urchin eggs and characterized its properties. We found that the native myosin VI was a monomeric and non-processive motor protein, and also showed that it moved toward the pointed end of F-actin. Ca2+ stimulated actin-activated MgATPase activity of the native myosin VI, while it lowered its motility on F-actin. Immunofluorescence microscopy showed that the myosin VI was translocated from the inner cytoplasm to the cortex after fertilization. Myosin VI may be involved in endocytic activities in fertilized eggs.

Key Words: F-actin, motor protein, myosin VI, sea urchin, unconventional myosin

Abbreviations: NP-40, Nonidet P-40; PMSF, phenylmethylsulfonyl fluoride; PVDF, polyvinylydene difluoride; TAME, N-p-tosyl-L-arginine methyl ester


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