Adaptability of myosin V studied by simultaneous detection of position and orientation.
We studied the structural dynamics of chicken myosin V by combining the localization power of fluorescent imaging with one nanometer accuracy (FIONA) with the ability to detect angular changes of a fluorescent probe. The myosin V was labeled with bifunctional rhodamine on one of its calmodulin light chains. For every 74 nm translocation, the probe exhibited two reorientational motions, associated with alternating smaller and larger translational steps. Molecules previously identified as stepping alternatively 74-0 nm were found to actually step 64-10 nm. Additional tilting often occurred without full steps, possibly indicating flexibility of the attached myosin heads or probing of their vicinity. Processive myosin V molecules sometimes shifted from the top to the side of actin, possibly to avoid an obstacle. The data indicate marked adaptability of this molecular motor to a nonuniform local environment and provide strong support for a straight-neck model of myosin V in which the lever arm of the leading head is tilted backwards at the prepowerstoke angle.
Syed
Sheyum
S
Department of Physics, University of Illinois, Urbana-Champaign, 61801, USA.
Snyder
Gregory E
GE
Franzini-Armstrong
Clara
C
Selvin
Paul R
PR
Goldman
Yale E
YE
D000199:Actins / Q000737:chemistry; D000818:Animals; D002147:Calmodulin / Q000737:chemistry; D002645:Chickens; D005454:Fluorescence Polarization; D020409:Molecular Motor Proteins / Q000737:chemistry; D024701:Myosin Type V / Q000737:chemistry* / Q000502:physiology*; D011487:Protein Conformation; D012235:Rhodamines / Q000737:chemistry
D000199:Actins; D002147:Calmodulin; D020409:Molecular Motor Proteins; D012235:Rhodamines; D024701:Myosin Type V