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Scientific article
English

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

Published inEMBO journal, vol. 21, no. 9, p. 2149-2158
Publication date2002
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.

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
Affiliation Not a UNIGE publication
Citation (ISO format)
HERM-GÖTZ, Angelika et al. Toxoplasma gondii myosin A and its light chain: a fast, single-headed, plus-end-directed motor. In: EMBO journal, 2002, vol. 21, n° 9, p. 2149–2158. doi: 10.1093/emboj/21.9.2149
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Article (Published version)
accessLevelRestricted
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ISSN of the journal0261-4189
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