Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction

J. E. T. Corrie, B. D. Brandmeier, R. E. Ferguson, D. R. Trentham, J. Kendrick-Jones, S. C. Hopkins, U. A. van der Heide, Y. E. Goldman, C. Sabido-David, R. E. Dale, S. Criddle and M. Irving ()
Additional contact information
J. E. T. Corrie: National Institute for Medical Research
B. D. Brandmeier: National Institute for Medical Research
R. E. Ferguson: National Institute for Medical Research
D. R. Trentham: National Institute for Medical Research
J. Kendrick-Jones: MRC Laboratory of Molecular Biology
S. C. Hopkins: Pennsylvania Muscle Institute, University of Pennsylvania
U. A. van der Heide: Pennsylvania Muscle Institute, University of Pennsylvania
Y. E. Goldman: Pennsylvania Muscle Institute, University of Pennsylvania
C. Sabido-David: Randall Institute, King's College London
R. E. Dale: Randall Institute, King's College London
S. Criddle: Randall Institute, King's College London
M. Irving: Randall Institute, King's College London

Nature, 1999, vol. 400, issue 6743, 425-430

Abstract: Abstract A new method is described for measuring motions of protein domains in their native environment on the physiological timescale. Pairs of cysteines are introduced into the domain at sites chosen from its static structure and are crosslinked by a bifunctional rhodamine. Domain orientation in a reconstituted macromolecular complex is determined by combining fluorescence polarization data from a small number of such labelled cysteine pairs. This approach bridges the gap between in vitro studies of protein structure and cellular studies of protein function and is used here to measure the tilt and twist of the myosin light-chain domain with respect to actin filaments in single muscle cells. The results reveal the structural basis for the lever-arm action of the light-chain domain of the myosin motor during force generation in muscle.

Date: 1999
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DOI: 10.1038/22704

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