Truncation of a mammalian myosin I results in loss of Ca2+-sensitive motility

Coluccio, Lynne M. and Perreault-Micale, Cynthia and Shushan, Alexander and Geeves, Michael A. (2000) Truncation of a mammalian myosin I results in loss of Ca2+-sensitive motility. Journal of Biological Chemistry, 275 (28). pp. 21618-21623. ISSN 0021-9258. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1074/jbc.M000363200

Abstract

MYR-1, a mammalian class I myosin, consisting of a heavy chain and 4–6 associated calmodulins, is represented by the 130-kDa myosin I (or MI130) from rat liver. MI130 translocates actin filaments in vitro in a Ca2+-regulated manner. A decrease in motility observed at higher Ca2+ concentrations has been attributed to calmodulin dissociation. To investigate mammalian myosin I regulation, we have coexpressed in baculovirus calmodulin and an epitope-tagged 85-kDa fragment representing the amino-terminal catalytic “motor” domain and the first calmodulin-binding IQ domain of ratmyr-1; we refer to this truncated molecule here as MI1IQ. Association of calmodulin to MI1IQ is Ca2+-insensitive. MI1IQ translocates actin filaments in vitro at a rate resembling MI130, but unlike MI130, does not exhibit sensitivity to 0.1–100 μm Ca2+. In addition to demonstrating successful expression of a functional truncated mammalian myosin Iin vitro, these results indicate that: 1) Ca2+-induced calmodulin dissociation from MI130in the presence of actin is not from the first IQ domain, 2) velocity is not affected by the length of the IQ region, and 3) the Ca2+ sensitivity of actin translocation exhibited by MI130 involves 1 or more of the other 5 IQ domains and/or the carboxyl tail.

Item Type: Article
Subjects: Q Science > Q Science (General)
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: P. Ogbuji
Date Deposited: 01 Apr 2009 16:52
Last Modified: 28 Apr 2014 13:45
Resource URI: http://kar.kent.ac.uk/id/eprint/16303 (The current URI for this page, for reference purposes)
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