NDLI: The neck region of the myosin motor domain acts as a lever arm to generate movement.

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The neck region of the myosin motor domain acts as a lever arm to generate movement.

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The neck region of the myosin motor domain acts as a lever arm to generate movement.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Uyeda, T. Q. Abramson, P. D. Spudich, J. A.
Description	Author Affiliation: Uyeda TQ ( National Institute for Advanced Interdisciplinary Research and Mechanical Engineering Laboratory, Agency of Industrial Science and Technology, Ibaraki, Japan.);
Abstract	The myosin head consists of a globular catalytic domain that binds actin and hydrolyzes ATP and a neck domain that consists of essential and regulatory light chains bound to a long alpha-helical portion of the heavy chain. The swinging neck-level model assumes that a swinging motion of the neck relative to the catalytic domain is the origin of movement. This model predicts that the step size, and consequently the sliding velocity, are linearly related to the length of the neck. We have tested this point by characterizing a series of mutant Dictyostelium myosins that have different neck lengths. The 2xELCBS mutant has an extra binding site for essential light chain. The delta RLCBS mutant myosin has an internal deletion that removes the regulatory light chain binding site. The delta BLCBS mutant lacks both light chain binding sites. Wild-type myosin and these mutant myosins were subjected to the sliding filament in vitro motility assay. As expected, mutants with shorter necks move slower than wild-type myosin in vitro. Most significantly, a mutant with a longer neck moves faster than the wild type, and the sliding velocities of these myosins are linearly related to the neck length, as predicted by the swinging neck-lever model. A simple extrapolation to zero speed predicts that the fulcrum point is in the vicinity of the SH1-SH2 region in the catalytic domain.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	93
Language	English
Publisher	National Academy of Sciences
Publisher Date	1996-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Models, Biological Myosins Chemistry Metabolism Physiology Protein Structure, Secondary Actins Adenosine Triphosphate Amino Acid Sequence Animals Binding Sites Ca(2+) Mg(2+)-ATPase Calcium-Transporting ATPases DNA Primers Dictyostelium Elasticity Kinetics Mathematics Molecular Sequence Data Muscle, Skeletal Mutagenesis, Site-Directed Biosynthesis Polymerase Chain Reaction Recombinant Proteins Sequence Homology, Amino Acid Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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