Transmission of force and displacement within the myosin molecule

Takashi Ohki, Sergey V. Mikhailenko, Manuel F. Morales, Hirofumi Onishi, Naoki Mochizuki

研究成果: Article査読

19 被引用数 (Scopus)

抄録

Myosin is a repetitive impeller of actin, using its catalysis of ATP hydrolysis to derive repeatedly the required free energy decrements. In each impulsion, changes at the myosin active site are transmitted through a series of structural elements to the myosin propeller (lever arm), almost 5 nm away. While the nature of transmission through most elements is evident, that through the so-called converter is not. To investigate how the converter changes linear displacement into rotation, we tested (one at a time) the effect of two Phe residue mutations (at 721 and 775) in the converter on the overall function of a heavy meromyosin (or subfragment 1) system, after first showing by observing kinetic behaviors that neither mutation affects other elements in the transmission. Using three tests (direct movement of the lever arm, activity in a motility assay with actin filaments, and direct force measurement of lever arm function), we found that these mutations affected only movements of the converter and the lever arm. From interpreting our observations in terms of the structure of the converter, we deduce that the linear-rotational transformation in the converter is mediated by a little machine (two Phe residues linked to a Gly) within a machine.

本文言語English
ページ(範囲)13707-13714
ページ数8
ジャーナルBiochemistry
43
43
DOI
出版ステータスPublished - 2004 11 2
外部発表はい

ASJC Scopus subject areas

  • Biochemistry

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