NDLI: Conformationally trapping the actin-binding cleft of myosin with a bifunctional spin label.

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Conformationally trapping the actin-binding cleft of myosin with a bifunctional spin label.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Moen, Rebecca J. Thomas, David D. Klein, Jennifer C.
Description	Author Affiliation: Moen RJ ( Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA.)
Abstract	We have trapped the catalytic domain of Dictyostelium (Dicty) myosin II in a weak actin-binding conformation by chemically crosslinking two engineered cysteines across the actin-binding cleft, using a bifunctional spin label (BSL). By connecting the lower and upper 50 kDa domains of myosin, the crosslink restricts the conformation of the actin-binding cleft. Crosslinking has no effect on the basal ATPase activity of isolated myosin, but it impairs rigor actin binding and actin-activation of myosin ATPase. EPR spectra of BSL provide insight into actomyosin structural dynamics. BSL is highly immobilized within the actin-binding cleft and is thus exquisitely sensitive to the global orientation and rotational motions of the myosin head. Conventional EPR shows that myosin heads bound to oriented actin filaments are highly disordered with respect to the actin filament axis, in contrast to the nearly crystalline order of myosin heads in rigor. This disorder is similar to that of weakly bound heads induced by ATP, but saturation transfer EPR shows that the disorder of crosslinked myosin is at least 100 times slower. Thus this cleft-crosslinked myosin is remarkably similar, in both actin affinity and rotational dynamics, to SH1-SH2 crosslinked BSL-myosin S1. We conclude that, whether myosin is trapped at the actin-myosin interface or in the force-generating region between the active site and lever arm, the structural state of myosin is intermediate between the weak-binding state preceding phosphate release and the strong-binding state that succeeds it. We propose that it represents the threshold of force generation.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	5
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Actins Metabolism Myosins Chemistry Spin Labels Actomyosin Animals Binding Sites Biomechanical Phenomena Catalytic Domain Cross-Linking Reagents Pharmacology Dictyostelium Drug Effects Electron Spin Resonance Spectroscopy Electrophoresis, Polyacrylamide Gel Models, Biological Protein Binding Protein Structure, Secondary Rabbits Rotation Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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