skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Constriction model of actomyosin ring for cytokinesis by fission yeast using a two-state sliding filament mechanism

Abstract

We developed a model describing the structure and contractile mechanism of the actomyosin ring in fission yeast, Schizosaccharomyces pombe. The proposed ring includes actin, myosin, and α-actinin, and is organized into a structure similar to that of muscle sarcomeres. This structure justifies the use of the sliding-filament mechanism developed by Huxley and Hill, but it is probably less organized relative to that of muscle sarcomeres. Ring contraction tension was generated via the same fundamental mechanism used to generate muscle tension, but some physicochemical parameters were adjusted to be consistent with the proposed ring structure. Simulations allowed an estimate of ring constriction tension that reproduced the observed ring constriction velocity using a physiologically possible, self-consistent set of parameters. Proposed molecular-level properties responsible for the thousand-fold slower constriction velocity of the ring relative to that of muscle sarcomeres include fewer myosin molecules involved, a less organized contractile configuration, a low α-actinin concentration, and a high resistance membrane tension. Ring constriction velocity is demonstrated as an exponential function of time despite a near linear appearance. We proposed a hypothesis to explain why excess myosin heads inhibit constriction velocity rather than enhance it. The model revealed how myosin concentration and elastic resistance tension aremore » balanced during cytokinesis in S. pombe.« less

Authors:
 [1];  [2]
  1. Department of Chemistry, Texas A and M University, College Station, Texas 77843-3255 (United States)
  2. Departments of Computer Science, Mathematics and Scientific Computing, and Graduate Program in Molecular Biophysics, Florida State University, Tallahassee, Florida 32306-4530 (United States)
Publication Date:
OSTI Identifier:
22308249
Resource Type:
Journal Article
Journal Name:
Journal of Chemical Physics
Additional Journal Information:
Journal Volume: 141; Journal Issue: 12; Other Information: (c) 2014 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0021-9606
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; ACTIN; FISSION; MOLECULES; MUSCLES; MYOSIN; SIMULATION; YEASTS

Citation Formats

Jung, Yong-Woon, and Mascagni, Michael. Constriction model of actomyosin ring for cytokinesis by fission yeast using a two-state sliding filament mechanism. United States: N. p., 2014. Web. doi:10.1063/1.4896164.
Jung, Yong-Woon, & Mascagni, Michael. Constriction model of actomyosin ring for cytokinesis by fission yeast using a two-state sliding filament mechanism. United States. https://doi.org/10.1063/1.4896164
Jung, Yong-Woon, and Mascagni, Michael. 2014. "Constriction model of actomyosin ring for cytokinesis by fission yeast using a two-state sliding filament mechanism". United States. https://doi.org/10.1063/1.4896164.
@article{osti_22308249,
title = {Constriction model of actomyosin ring for cytokinesis by fission yeast using a two-state sliding filament mechanism},
author = {Jung, Yong-Woon and Mascagni, Michael},
abstractNote = {We developed a model describing the structure and contractile mechanism of the actomyosin ring in fission yeast, Schizosaccharomyces pombe. The proposed ring includes actin, myosin, and α-actinin, and is organized into a structure similar to that of muscle sarcomeres. This structure justifies the use of the sliding-filament mechanism developed by Huxley and Hill, but it is probably less organized relative to that of muscle sarcomeres. Ring contraction tension was generated via the same fundamental mechanism used to generate muscle tension, but some physicochemical parameters were adjusted to be consistent with the proposed ring structure. Simulations allowed an estimate of ring constriction tension that reproduced the observed ring constriction velocity using a physiologically possible, self-consistent set of parameters. Proposed molecular-level properties responsible for the thousand-fold slower constriction velocity of the ring relative to that of muscle sarcomeres include fewer myosin molecules involved, a less organized contractile configuration, a low α-actinin concentration, and a high resistance membrane tension. Ring constriction velocity is demonstrated as an exponential function of time despite a near linear appearance. We proposed a hypothesis to explain why excess myosin heads inhibit constriction velocity rather than enhance it. The model revealed how myosin concentration and elastic resistance tension are balanced during cytokinesis in S. pombe.},
doi = {10.1063/1.4896164},
url = {https://www.osti.gov/biblio/22308249}, journal = {Journal of Chemical Physics},
issn = {0021-9606},
number = 12,
volume = 141,
place = {United States},
year = {Sun Sep 28 00:00:00 EDT 2014},
month = {Sun Sep 28 00:00:00 EDT 2014}
}