ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy

Hernando Sosa, Erwin J.G. Peterman, W. E. Moerner, Lawrence S.B. Goldstein

Research output: Contribution to journalArticle

121 Scopus citations

Abstract

Kinesin is an ATP-driven molecular motor protein that moves processively along microtubules. Despite considerable research, the detailed mechanism of kinesin motion remains elusive. We applied an enhanced suite of single- and multiple-molecule fluorescence polarization microscopy assays to report the orientation and mobility of kinesin molecules bound to microtubules as a function of nucleotide state. In the presence of analogs of ATP, ADP-Pi or in the absence of nucleotide, the kinesin head maintains a rigid orientation. In the presence of ADP, the motor domain of kinesin, still bound to the microtubule, adopts a previously undescribed, highly mobile state. This state may be general to the chemomechanical cycle of motor proteins; in the case of kinesin, the transition from a highly mobile to a rigid state after ADP release may contribute to the generation of the 8 nm step.

Original languageEnglish (US)
Pages (from-to)540-544
Number of pages5
JournalNature structural biology
Volume8
Issue number6
DOIs
StatePublished - Jun 21 2001

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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