Coulton, A.T. and Skoumpla, K. and Lehman, W. and Geeves, M.A. and Mulvihill, D.P. (2007) Acetylation regulates tropomyosin function in the fission yeast Schizosaccharomyces pombe. Journal of Cell Science, 120 (9). pp. 1635-1645. ISSN 0021-9533.
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Tropomyosin is an evolutionarily conserved alpha-helical coiled-coil protein that promotes and maintains actin filaments. In yeast, Tropomyosin-stabilised filaments are used by molecular motors to transport cargoes or to generate motile forces by altering the dynamics of filament growth and shrinkage. The Schizosaccharomyces pombe tropomyosin Cdc8 localises to the cytokinetic actomyosin ring during mitosis and is absolutely required for its formation and function. We show that Cdc8 associates with actin filaments throughout the cell cycle and is subjected to post-translational modification that does not vary with cell cycle progression. At any given point in the cell cycle 80% of Cdc8 molecules are acetylated, which significantly enhances their affinity for actin. Reconstructions of electron microscopic images of actin-Cdc8 filaments establish that the majority of Cdc8 strands sit in the 'closed' position on actin filaments, suggesting a role in the regulation of myosin binding. We show that Cdc8 regulates the equilibrium binding of myosin to actin without affecting the rate of myosin binding. Unacetylated Cdc8 isoforms bind actin, but have a reduced ability to regulate myosin binding to actin. We conclude that although acetylation of Cdc8 is not essential, it provides a regulatory mechanism for modulating actin filament integrity and myosin function.
|Uncontrolled keywords:||acetylation; actin; tropomyosin; Cdc8; Schizosaccharomyces pombe; fission yeast|
|Subjects:||Q Science > QR Microbiology|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences > Cell & Developmental Biology Group|
|Depositing User:||Stephen Holland|
|Date Deposited:||19 Dec 2007 18:56|
|Last Modified:||14 Jan 2010 14:03|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/1423 (The current URI for this page, for reference purposes)|
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