Actomyosin motility on nanostructured surfaces.

We have here, for the first time, used nanofabrication techniques to reproduce aspects of the ordered actomyosin arrangement in a muscle cell. The adsorption of functional heavy meromyosin (HMM) to five different resist polymers was first assessed. One group of resists (MRL-6000.1XP and ZEP-520) consistently exhibited high quality motility of actin filaments after incubation with HMM. A second group (PMMA-200, PMMA-950, and MRI-9030) generally gave low quality of motility with only few smoothly moving filaments. Based on these findings electron beam lithography was applied to a bi-layer resist system with PMMA-950 on top of MRL-6000.1XP. Grooves (100-200nm wide) in the PMMA layer were created to expose the MRL-6000.1XP surface for adsorption of HMM and guidance of actin filament motility. This guidance was quite efficient allowing no U-turns of the filaments and approximately 20 times higher density of moving filaments in the grooves than on the surrounding PMMA.

[1]  D V Nicolau,et al.  Actin motion on microlithographically functionalized myosin surfaces and tracks. , 1999, Biophysical journal.

[2]  Toshio Yanagida,et al.  Sliding movement of single actin filaments on one-headed myosin filaments , 1987, Nature.

[3]  Toshio Yanagida,et al.  Force measurements by micromanipulation of a single actin filament by glass needles , 1988, Nature.

[4]  H. Yamashita,et al.  Dynamic interaction between cardiac myosin isoforms modifies velocity of actomyosin sliding in vitro. , 1993, Circulation research.

[5]  J. Spudich,et al.  Assays for actin sliding movement over myosin-coated surfaces. , 1991, Methods in enzymology.

[6]  K. Trybus,et al.  Coiled-coil unwinding at the smooth muscle myosin head-rod junction is required for optimal mechanical performance. , 2001, Biophysical journal.

[7]  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.

[8]  S. Mashiko,et al.  Control of actin moving trajectory by patterned poly(methylmethacrylate) tracks. , 1997, Biophysical journal.

[9]  T. Yanagida,et al.  Orientation dependence of displacements by a single one-headed myosin relative to the actin filament. , 1998, Biophysical journal.

[10]  T Kanayama,et al.  Controlling the direction of kinesin-driven microtubule movements along microlithographic tracks. , 2001, Biophysical journal.

[11]  James A. Spudich,et al.  A myosin II mutation uncouples ATPase activity from motility and shortens step size , 2001, Nature Cell Biology.

[12]  M. Geeves,et al.  Cooperativity between the two heads of rabbit skeletal muscle heavy meromyosin in binding to actin. , 1998, Biophysical journal.

[13]  E. Katayama,et al.  Cooperativity between two heads of dictyostelium myosin II in in vitro motility and ATP hydrolysis. , 1999, Biophysical journal.

[14]  Daniel Safer,et al.  Myosin VI is an actin-based motor that moves backwards , 1999, Nature.

[15]  A. Månsson,et al.  Multivariate statistics in analysis of data from the in vitro motility assay. , 2003, Analytical biochemistry.

[16]  James A. Spudich,et al.  Chapter 18 Purification of Muscle Actin , 1982 .

[17]  A. Somlyo,et al.  Signal transduction by G‐proteins, Rho‐kinase and protein phosphatase to smooth muscle and non‐muscle myosin II , 2000, The Journal of physiology.

[18]  J. Burns,et al.  Single-molecule mechanics of heavy meromyosin and S1 interacting with rabbit or Drosophila actins using optical tweezers. , 1995, Biophysical journal.

[19]  E. Homsher,et al.  Calcium regulation of thin filament movement in an in vitro motility assay. , 1996, Biophysical journal.

[20]  C. Berger,et al.  ADP Binding Induces an Asymmetry between the Heads of Unphosphorylated Myosin* , 2001, The Journal of Biological Chemistry.

[21]  T. Yanagida,et al.  Subpiconewton intermolecular force microscopy. , 1997, Biochemical and biophysical research communications.

[22]  A. Arner,et al.  Cardiotonic bipyridine amrinone slows myosin-induced actin filament sliding at saturating [MgATP] , 2004, Journal of Muscle Research & Cell Motility.

[23]  Frank Jülicher,et al.  Acting on actin: the electric motility assay , 1999, European Biophysics Journal.

[24]  J. Spudich,et al.  Bidirectional movement of actin filaments along tracks of myosin heads , 1989, Nature.

[25]  K. Trybus,et al.  Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro , 1990, The Journal of cell biology.

[26]  J. D. Pardee,et al.  [18] Purification of muscle actin , 1982 .

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