Configuration of the two kinesin motor domains during ATP hydrolysis.
To understand the mechanism of kinesin movement we have investigated the relative configuration of the two kinesin motor domains during ATP hydrolysis using fluorescence polarization microscopy of ensemble and single molecules. We found that: (i) in nucleotide states that induce strong microtubule binding, both motor domains are bound to the microtubule with similar orientations; (ii) this orientation is maintained during processive motion in the presence of ATP; (iii) the neck-linker region of the motor domain has distinct configurations for each nucleotide condition tested. Our results fit well with a hand-over-hand type movement mechanism and suggest how the ATPase cycle in the two motor domains is coordinated. We propose that the motor neck-linker domain configuration controls ADP release.
Asenjo
Ana B
AB
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Krohn
Natan
N
Sosa
Hernando
H
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism*; D019281:Dimerization; D006801:Humans; D016547:Kinesins / Q000378:metabolism*; D015335:Molecular Probes; D017434:Protein Structure, Tertiary; D021381:Protein Transport
D015335:Molecular Probes; D000255:Adenosine Triphosphate; D016547:Kinesins