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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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WRAP-Steric-hindrance-in-the-upper-50-kDa-domain-Palani-2018.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution. Download (8Mb) | Preview |
Official URL: http://dx.doi.org/10.1242/jcs.205625
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 | |||||||||||||||||||||
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| Subjects: | Q Science > QH Natural history > QH301 Biology Q Science > QP Physiology |
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| Divisions: | Faculty of Medicine > Warwick Medical School > Biomedical Sciences Faculty of Medicine > Warwick Medical School |
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| 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: |
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| Date of first compliant deposit: | 12 June 2018 | |||||||||||||||||||||
| 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: |
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