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 language | English (US) |
|---|---|
| Pages (from-to) | 540-544 |
| Number of pages | 5 |
| Journal | Nature Structural Biology |
| Volume | 8 |
| Issue number | 6 |
| DOIs | |
| State | Published - 2001 |
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ASJC Scopus subject areas
- Biochemistry
- Structural Biology
- Genetics
Cite this
ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy. / Sosa, Hernando J.; Peterman, Erwin J G; Moerner, W. E.; Goldstein, Lawrence S B.
In: Nature Structural Biology, Vol. 8, No. 6, 2001, p. 540-544.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy
AU - Sosa, Hernando J.
AU - Peterman, Erwin J G
AU - Moerner, W. E.
AU - Goldstein, Lawrence S B
PY - 2001
Y1 - 2001
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0034995132&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034995132&partnerID=8YFLogxK
U2 - 10.1038/88611
DO - 10.1038/88611
M3 - Article
C2 - 11373624
AN - SCOPUS:0034995132
VL - 8
SP - 540
EP - 544
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
SN - 1545-9993
IS - 6
ER -