Molecular motors: force and movement generated by single myosin II molecules.

Muscle myosin II is an ATP-driven, actin-based molecular motor. Recent developments in optical tweezers technology have made it possible to study movement and force production on the single-molecule level and to find out how different myosin isoforms may have adapted to their specific physiological roles.

[1]  M. Geeves,et al.  Interaction of actin and ADP with the head domain of smooth muscle myosin: implications for strain-dependent ADP release in smooth muscle. , 1998, Biochemistry.

[2]  S M Block,et al.  Fifty Ways to Love Your Lever: Myosin Motors , 1996, Cell.

[3]  A. Somlyo,et al.  MgADP promotes a catch-like state developed through force-calcium hysteresis in tonic smooth muscle. , 1998, Biophysical journal.

[4]  J. Sellers,et al.  Myosins: a diverse superfamily. , 2000, Biochimica et biophysica acta.

[5]  J. Spudich,et al.  Single myosin molecule mechanics: piconewton forces and nanometre steps , 1994, Nature.

[6]  W H Guilford,et al.  Two heads of myosin are better than one for generating force and motion. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[7]  R. T. Tregear,et al.  Movement and force produced by a single myosin head , 1995, Nature.

[8]  Dietmar J. Manstein,et al.  Single-molecule tracking of myosins with genetically engineered amplifier domains , 2001, Nature Structural Biology.

[9]  M. Siegman,et al.  The myosin cross-bridge cycle and its control by twitchin phosphorylation in catch muscle. , 2001, Biophysical journal.

[10]  Steven M. Block.  Fifty Ways to Love Your Lever: Review Myosin Motors , 1996 .

[11]  M. Geeves,et al.  Transient Kinetic Analysis of the 130-kDa Myosin I (MYR-1 Gene Product) from Rat Liver , 1999, The Journal of Biological Chemistry.

[12]  Justin E. Molloy,et al.  The motor protein myosin-I produces its working stroke in two steps , 1999, Nature.

[13]  A. Huxley.  Mechanics and models of the myosin motor. , 2000, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[14]  Michael Whittaker,et al.  A 35-Å movement of smooth muscle myosin on ADP release , 1995, Nature.

[15]  K C Holmes,et al.  Structural mechanism of muscle contraction. , 1999, Annual review of biochemistry.

[16]  Roberto Dominguez,et al.  Crystal Structure of a Vertebrate Smooth Muscle Myosin Motor Domain and Its Complex with the Essential Light Chain Visualization of the Pre–Power Stroke State , 1998, Cell.

[17]  R A Milligan,et al.  Structure of the actin-myosin complex and its implications for muscle contraction. , 1993, Science.

[18]  R. Milligan,et al.  Brush Border Myosin–I Structure and ADP-dependent Conformational Changes Revealed by Cryoelectron Microscopy and Image Analysis , 1997, The Journal of cell biology.

[19]  Hiroto Tanaka,et al.  Simultaneous Observation of Individual ATPase and Mechanical Events by a Single Myosin Molecule during Interaction with Actin , 1998, Cell.

[20]  Toshio Yanagida,et al.  A single myosin head moves along an actin filament with regular steps of 5.3 nanometres , 1999, Nature.

[21]  C. Veigel,et al.  An unexpectedly large working stroke from chymotryptic fragments of myosin II , 2000, FEBS letters.