Detection of sub-8-nm movements of kinesin by high-resolution optical-trap microscopy

被引:99
作者
Coppin, CM
Finer, JT
Spudich, JA
Vale, RD
机构
[1] UNIV CALIF SAN FRANCISCO,HOWARD HUGHES MED INST,SAN FRANCISCO,CA 94143
[2] STANFORD UNIV,SCH MED,BECKMAN CTR,DEPT BIOCHEM,STANFORD,CA 94305
[3] STANFORD UNIV,SCH MED,BECKMAN CTR,DEPT BIOL,STANFORD,CA 94305
关键词
D O I
10.1073/pnas.93.5.1913
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 [理学]; 0710 [生物学]; 09 [农学];
摘要
Kinesin is a molecular motor that transports organelles along microtubules. This enzyme has two identical 7-nm-long motor domains, which it uses to move between consecutive tubulin binding sites spaced 8 nm apart along a microtubular protofilament. The molecular mechanism of this movement, which remains to be elucidated, may be common to all families of motor proteins, In this study, a high-resolution optical-trap microscope was used to measure directly the magnitude of abrupt displacements produced by a single kinesin molecule transporting a microscopic bead, The distribution of magnitudes reveals that kinesin not only undergoes discrete 8-nm movements, in agreement with previous work [Svoboda, K., Schmidt, C. F., Schnapp, B. J. & Block, S.M. (1993) Nature (London) 365, 721-727], but also frequently exhibits smaller movements of about 5 nm. A possible explanation for these unexpected smaller movements is that kinesin's movement from one dimer to the next along a protofilament involves at least two distinct events in the mechanical cycle.
引用
收藏
页码:1913 / 1917
页数:5
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