An unexpectedly large working stroke from chymotryptic fragments of myosin II.
Recent structural evidence indicates that the light chain domain of the myosin head (LCD) bends on the motor domain (MD) to move actin. Structural models usually assume that the actin-MD interface remains static and the possibility that part of the myosin working stroke might be produced by rotation about the acto-myosin interface has been neglected. We have used an optical trap to measure the movement produced by proteolytically shortened single rabbit skeletal muscle myosin heads (S-1(A1) and S-1(A2)). The working stroke produced by these shortened heads was more than that which the MD-LCD bend mechanism predicts from the full-length (papain) S-1's working stroke obtained under similar conditions. This result indicates that part of the working stroke may be caused by motor action at the actin-MD interface.
Molloy
J E
JE
Department of Biology, University of York, UK.
Kendrick-Jones
J
J
Veigel
C
C
Tregear
R T
RT
D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002918:Chymotrypsin / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D011817:Rabbits
D000199:Actins; D010446:Peptide Fragments; D000255:Adenosine Triphosphate; D002918:Chymotrypsin; D009218:Myosins