Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle.
Force generation and relative sliding between the myosin and actin filaments in muscle are thought to be caused by tilting of the head region of the myosin crossbridges between the filaments. Structural and spectroscopic experiments have demonstrated segmental flexibility of myosin in muscle, but have not shown a direct linkage between tilting of the myosin heads and either force generation or filament sliding. Here we use fluorescence polarization to detect changes in the orientation of the light-chain region of the head, the part most likely to tilt, and synchronized head movements by imposing rapid length steps. We found that the light-chain region of the myosin head tilts both during the imposed filament sliding and during the subsequent quick force recovery that is thought to signal the elementary force-generating event.
Irving
M
M
Randall Institute, King's College London, UK.
St Claire Allen
T
T
Sabido-David
C
C
Craik
J S
JS
Brandmeier
B
B
Kendrick-Jones
J
J
Corrie
J E
JE
Trentham
D R
DR
Goldman
Y E
YE
D000818:Animals; D001696:Biomechanical Phenomena; D002645:Chickens; D004926:Escherichia coli; D005454:Fluorescence Polarization; D066298:In Vitro Techniques; D009119:Muscle Contraction / Q000502:physiology*; D018482:Muscle, Skeletal / Q000502:physiology*; D009218:Myosins / Q000502:physiology*; D011817:Rabbits; D011994:Recombinant Proteins; D012235:Rhodamines; D012518:Sarcomeres / Q000502:physiology
D011994:Recombinant Proteins; D012235:Rhodamines; D009218:Myosins