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Steric hindrance in the upper 50 kDa domain of the motor Myo2p leads to cytokinesis defects in fission yeast

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Palani, Saravanan, Srinivasan, Rajagopalan, Zambon, Paola, Kamnev, Anton, Gayathri, Pananghat and Balasubramanian, Mohan K. (2018) Steric hindrance in the upper 50 kDa domain of the motor Myo2p leads to cytokinesis defects in fission yeast. Journal of Cell Science, 131 (1). jcs205625. doi:10.1242/jcs.205625

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Official URL: http://dx.doi.org/10.1242/jcs.205625

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Abstract

Cytokinesis in many eukaryotes requires a contractile actomyosin ring that is placed at the division site. In fission yeast, which is an attractive organism for the study of cytokinesis, actomyosin ring assembly and contraction requires the myosin II heavy chain Myo2p. Although myo2-E1, a temperature-sensitive mutant defective in the upper 50 kDa domain of Myo2p, has been studied extensively, the molecular basis of the cytokinesis defect is not understood. Here, we isolate myo2-E1-Sup2, an intragenic suppressor that contains the original mutation in myo2-E1 (G345R) and a second mutation in the upper 50 kDa domain (Y297C). Unlike myo2-E1-Sup1, a previously characterized myo2-E1 suppressor, myo2-E1-Sup2 reverses actomyosin ring contraction defects in vitro and in vivo. Structural analysis of available myosin motor domain conformations suggests that a steric clash in myo2-E1, which is caused by the replacement of a glycine with a bulky arginine, is relieved in myo2-E1-Sup2 by mutation of a tyrosine to a smaller cysteine. Our work provides insight into the function of the upper 50 kDa domain of Myo2p, informs a molecular basis for the cytokinesis defect in myo2-E1, and may be relevant to the understanding of certain cardiomyopathies.

Item Type: Journal Article
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences
Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH): Cytokinesis -- Molecular aspects, Actomyosin
Journal or Publication Title: Journal of Cell Science
Publisher: The Company of Biologists Ltd.
ISSN: 1477-9137
Official Date: 4 January 2018
Dates:
DateEvent
4 January 2018Published
11 November 2017Accepted
Volume: 131
Number: 1
Article Number: jcs205625
DOI: 10.1242/jcs.205625
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
UNSPECIFIEDWarwick Medical Schoolhttp://dx.doi.org/10.13039/501100004443
UNSPECIFIED[RS] Royal Societyhttp://dx.doi.org/10.13039/501100000288
WT101885MAWellcome Trusthttp://dx.doi.org/10.13039/100010269
Actomyosin ring no. 671083European Research Council [ERC]http://viaf.org/viaf/130022607
INSPIREDepartment of Biotechnology, Ministry of Science and Technologyhttp://dx.doi.org/10.13039/501100001407
Innovative young Biotechnologist Award (IYBA)Department of Biotechnology, Ministry of Science and Technologyhttp://dx.doi.org/10.13039/501100001407

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