Toxoplasma gondii myosin A and its light chain: a fast, single-headed, plus-end-directed motor

Herm-Gotz, Angelika and Weiss, Stefan and Stratmann, Rolf and Fujita-Becker, Setsuko and Ruff, Christine and Meyhofer, Edgar and Soldati, Thierry and Manstein, Dietmar J. and Geeves, Michael A. and Soldati, Dominique (2002) Toxoplasma gondii myosin A and its light chain: a fast, single-headed, plus-end-directed motor. EMBO Journal, 21 (9). pp. 2149-2158. ISSN 0261-4189 . (The full text of this publication is not available from this repository)

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Abstract

Successful host cell invasion is a prerequisite for survival of the obligate intracellular apicomplexan parasites and establishment of infection. Toxoplasma gondii penetrates host cells by an active process involving its own actomyosin system and which is distinct from induced phagocytosis. Toxoplasma gondii myosin A (TgMyoA) is presumed to achieve power gliding motion and host cell penetration by the capping of apically released adhesins towards the rear of the parasite. We report here an extensive biochemical characterization of the functional TgMyoA motor complex. TgMyoA is anchored at the plasma membrane and binds a novel type of myosin light chain (TgMLC1). Despite some unusual features, the kinetic and mechanical properties of TgMyoA are unexpectedly similar to those of fast skeletal muscle myosins. Microneedle-laser trap and sliding velocity assays established that TgMyoA moves in unitary steps of 5.3 nm with a velocity of 5.2 microm/s towards the plus end of actin filaments. TgMyoA is the first fast, single-headed myosin and fulfils all the requirements for power parasite gliding.

Item Type: Article
Additional information: 0261-4189 (Print) Journal Article Research Support, Non-U.S. Gov't
Uncontrolled keywords: Amino Acid Sequence Animals Kinetics *Molecular Motor Proteins Molecular Sequence Data Myosin Light Chains/*physiology Nonmuscle Myosin Type IIA/*physiology Sequence Alignment Toxoplasma/*physiology
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Michael Geeves
Date Deposited: 04 Sep 2008 15:01
Last Modified: 21 May 2014 07:34
Resource URI: http://kar.kent.ac.uk/id/eprint/4007 (The current URI for this page, for reference purposes)
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