Stepwise Motion of an Actin Filament over a Small Number of Heavy Meromyosin Molecules Is Revealed in an In Vitro Motility Assay1

1994 ◽  
Vol 115 (4) ◽  
pp. 644-647 ◽  
Author(s):  
Hidetake Miyata ◽  
Hiroyuki Hakozaki ◽  
Hiroshi Yoshikawa ◽  
Naoya Suzuki ◽  
Kazuhiko Kinosita ◽  
...  
2019 ◽  
Vol 116 (35) ◽  
pp. 17336-17344 ◽  
Author(s):  
Zsombor Balassy ◽  
Anne-Marie Lauzon ◽  
Lennart Hilbert

Global changes in the state of spatially distributed systems can often be traced back to perturbations that arise locally. Whether such local perturbations grow into global changes depends on the system geometry and the spatial spreading of these perturbations. Here, we investigate how different spreading behaviors of local perturbations determine their global impact in 1-dimensional systems of different size. Specifically, we assessed sliding arrest events in in vitro motility assays where myosins propel actin, and simulated the underlying mechanochemistry of myosins that bind along the actin filament. We observed spontaneous sliding arrest events that occurred more frequently for shorter actin filaments. This observation could be explained by spontaneous local arrest of myosin kinetics that stabilizes once it spreads throughout an entire actin filament. When we introduced intermediate concentrations of the actin cross-linker filamin, longer actin was arrested more frequently. This observation was reproduced by simulations where filamin binding induces persistent local arrest of myosin kinetics, which subsequently spreads throughout the actin filament. A spin chain model with nearest-neighbor coupling reproduced key features of our experiments and simulations, thus extending to other linear systems with nearest-neighbor coupling the following conclusions: 1) perturbations that are persistent only once they spread throughout the system are more effective in smaller systems, and 2) perturbations that are persistent upon their establishment are more effective in larger systems. Beyond these general conclusions, our work also provides a theoretical model of collective myosin kinetics with a finite range of mechanical coupling along the actin filament.


1999 ◽  
Vol 273 (1) ◽  
pp. 12-19 ◽  
Author(s):  
W. Hamelink ◽  
J.G. Zegers ◽  
B.W. Treijtel ◽  
T. Blangé

2008 ◽  
Vol 40 (Supplement) ◽  
pp. S297
Author(s):  
Hideyo Takatsuki ◽  
Kevin M. Rice ◽  
Shinichi Asano ◽  
Devashish Desai ◽  
Madhukar Kolli ◽  
...  

2011 ◽  
Vol 100 (3) ◽  
pp. 128a-129a
Author(s):  
Edward P. Debold ◽  
Matthew Turner ◽  
Jordan C. Stout ◽  
Samuel C. Walcott

Biosystems ◽  
2011 ◽  
Vol 103 (1) ◽  
pp. 79-84 ◽  
Author(s):  
Itsuki Kunita ◽  
Shigeru Sakurazawa ◽  
Hajime Honda

PLoS ONE ◽  
2017 ◽  
Vol 12 (7) ◽  
pp. e0181171 ◽  
Author(s):  
Kohei Iwase ◽  
Masateru Tanaka ◽  
Keiko Hirose ◽  
Taro Q. P. Uyeda ◽  
Hajime Honda

2001 ◽  
Vol 280 (2) ◽  
pp. C309-C316 ◽  
Author(s):  
Thomas J. Eddinger ◽  
Daniel P. Meer

Isolated single smooth muscle cells (SMCs) from different regions of the rabbit stomach were used to determine a possible correlation between unloaded shortening velocity and smooth muscle (SM) myosin heavy chain (MHC) S1 head isoform composition (SMA, no head insert; SMB, with head insert). α-Toxin-permeabilized isolated single cells were maximally activated to measure unloaded shortening velocity and subsequently used in an RT-PCR reaction to determine the SMA/SMB content of the same cell. SM MHC SMA and SMB isoforms are uniquely distributed in the stomach with cells from the fundic region expressing little SMB (38.1 ± 7.3% SMB; n = 16); cells from the antrum express primarily SMB (94.9 ± 1.0% SMB; n = 16). Mean fundic cell unloaded shortening velocity was 0.014 ± 0.002 cell lengths/s compared with 0.036 ± 0.002 for the antrum cells. Unloaded shortening velocity in these cells was significantly correlated with their percent SMB expression ( r 2 = 0.58). Resting cell length does not correlate with the percent SMB expression ( n = 32 cells). Previously published assays of purified or expressed SMA and SMB heavy meromyosin show a twofold difference in actin filament sliding speed in in vitro motility assays. Extrapolation of our data to 0–100% SMB would give a 10-fold range of shortening velocity, which is closer to the ∼20-fold range reported from various SM tissues. This suggests that mechanisms in addition to the MHC S1 head isoforms regulate shortening velocity.


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