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Two single-headed myosin V motors bound to a tetrameric adapter protein form a processive complex.

Myo4p, one of two class V myosins in budding yeast, continuously transports messenger RNA (mRNA) cargo in the cell but is nonprocessive when characterized in vitro. The adapter protein She3p tightly binds to the Myo4p rod, forming a single-headed motor complex. In this paper, we show that two Myo4p-She3p motors are recruited by the tetrameric mRNA-binding protein She2p to form a processive double-headed complex. The binding site for She3p was mapped to a single α helix that protrudes at right angles from She2p. Processive runs of several micrometers on yeast actin-tropomyosin filaments were observed only in the presence of She2p, and, thus, motor activity is regulated by cargo binding. While moving processively, each head steps ~72 nm in a hand-over-hand motion. Coupling two high-duty cycle monomeric motors via a common cargo-binding adapter protein creates a complex with transport properties comparable with a single dimeric processive motor such as vertebrate myosin Va.

Pubmed ID: 22084309


  • Krementsova EB
  • Hodges AR
  • Bookwalter CS
  • Sladewski TE
  • Travaglia M
  • Sweeney HL
  • Trybus KM


The Journal of cell biology

Publication Data

November 14, 2011

Associated Grants

  • Agency: NIAMS NIH HHS, Id: AR35661
  • Agency: NIGMS NIH HHS, Id: GM078097
  • Agency: NIGMS NIH HHS, Id: R01 GM078097

Mesh Terms

  • Models, Molecular
  • Myosin Heavy Chains
  • Myosin Type V
  • Protein Conformation
  • RNA, Messenger
  • RNA-Binding Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins