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An unexpectedly large working stroke from chymotryptic fragments of myosin II
[摘要]

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.

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[关键词] Myosin;Working stroke;Optical trap;Motor;Muscle;Single molecule;MD;motor domain;LCD;light chain binding domain;S-1;subfragment 1;the digestion product containing the motor head of myosin;S-1(A1);S-1(A2);the chymotryptically derived motor head isoenzymes;ELC;essential light chain;RLC;regulatory light chain [时效性] 
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