Strength and lifetime of the bond between actin and skeletal muscle α-actinin studied with an optical trapping technique

Hidetake Miyata*, Ryohei Yasuda, Kazuhiko Kinosita

*この研究の対応する著者

研究成果: Article査読

66 被引用数 (Scopus)

抄録

The force required to break the bond between skeletal muscle actin and α-actinin (unbinding force) was measured at the level of individual molecules with an optical trapping technique. An actin filament, to the barbed-end of which was attached a gelsolin-coated polystyrene bead, was bound to α-actinin molecules adsorbed to a nitrocellulose-coated glass surface (~ 1 α-actinin molecule per 1 μm actin filament). The filament-bound bead was held by the optical trap and the force was applied to break the bond by pulling the bead. The unbinding force ranged from 1.4 to 44 pN. The average magnitude of the force was ~ 18 pN. As the probability of the bond breakage has been suggested to be governed by the magnitude of the external force, the relationship was studied between the magnitude of the unbinding force and the time required to break the bond (unbinding time). The unbinding time ranged from ~ 0.1 to ~ 20 seconds, and tended to become shorter as the unbinding force became larger. The unbinding time seemed to be classifiable into two major groups: one group having a time value of 1 sec or less and the other having a time value ranging from several to 20 seconds. This suggests the existence of at least two classes of the actin-actinin bonds.

本文言語English
ページ(範囲)83-88
ページ数6
ジャーナルBiochimica et Biophysica Acta - General Subjects
1290
1
DOI
出版ステータスPublished - 1996 5 21
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 生物理学
  • 分子生物学

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