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PMID: 7791902 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle.

Nature ·Vol. 375 ·No. 6533 ·1995-06-22 ·Pages 688-91

Irving M, St Claire Allen T, Sabido-David C, Craik JS, Brandmeier B, Kendrick-Jones J, Corrie JE, Trentham DR, Goldman YE

Abstract

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.

MeSH Terms
Animals Biomechanical Phenomena Chickens Escherichia coli Fluorescence Polarization In Vitro Techniques Muscle Contraction/physiology Muscle, Skeletal/physiology Myosins/physiology Rabbits Recombinant Proteins Rhodamines Sarcomeres/physiology
Chemicals
Recombinant Proteins Rhodamines Myosins
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Irving M
Randall Institute, King's College London, UK.
St Claire Allen T
Sabido-David C
Craik J S
Brandmeier B
Kendrick-Jones J
Corrie J E
Trentham D R
Goldman Y E
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1995-06-22
Pages
688-91
Language
English
Region
England
NLM ID
0410462
Subset
IM
Grants
Wellcome Trust · United Kingdom
Corrections
CommentIn
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