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

Herm-Götz, A., Weiss, S., Stratmann, R., Fujita-Becker, S., Ruff, C., Meyhöfer, E., et al. (2002). Toxoplasma gondii myosin A and its light chain: a fast, single‐headed, plus‐end‐directed motor. The EMBO Journal, 21(9), 2149-2158. doi:10.1093/emboj/21.9.2149.

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Genre: Journal Article
Alternative Title : Toxoplasma gondii myosin A and its light chain: a fast, single‐headed, plus‐end‐directed motor

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EMBOJ_21_2002_2149.pdf (Any fulltext), 411KB
 
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 Creators:
Herm-Götz, Angelika, Author
Weiss, Stefan, Author
Stratmann, Rolf, Author
Fujita-Becker, Setsuko1, Author              
Ruff, Christine, Author
Meyhöfer, Edgar, Author
Soldati, Thierry2, Author              
Manstein, Dietmar J.1, Author              
Geeves, Michael A., Author
Soldati, Dominique, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              

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Free keywords: invasion; myosin; myosin light chain; Toxoplasma gondii; transient kinetics
 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.

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Language(s): eng - English
 Dates: 2002-02-262001-12-122002-03-082002-05-012002-05-01
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: The EMBO Journal
Source Genre: Journal
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Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 21 (9) Sequence Number: - Start / End Page: 2149 - 2158 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061_1