Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/4003
Full metadata record
DC FieldValueLanguage
dc.contributor.authorPalani, Saravananen_US
dc.contributor.authorSrinivasan, Ramanujamen_US
dc.contributor.authorZambon, Paolaen_US
dc.contributor.authorKamnev, Antonen_US
dc.contributor.authorPANANGHAT, GAYATHRIen_US
dc.date.accessioned2019-09-09T11:37:14Z
dc.date.available2019-09-09T11:37:14Z
dc.date.issued2018-01en_US
dc.identifier.citationJournal of Cell Science, 131, jcs205625.en_US
dc.identifier.issn0021-9533en_US
dc.identifier.issn1477-9137en_US
dc.identifier.urihttp://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/4003-
dc.identifier.urihttps://doi.org/10.1242/jcs.205625en_US
dc.description.abstractCytokinesis 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.en_US
dc.language.isoenen_US
dc.publisherThe Company of Biologists Ltden_US
dc.subjectActomyosin ringen_US
dc.subjectCytokinesisen_US
dc.subjectFission yeasten_US
dc.subjectMyosinen_US
dc.subject2018en_US
dc.titleSteric hindrance in the upper 50 kDa domain of the motor Myo2p leads to cytokinesis defects in fission yeasten_US
dc.typeArticleen_US
dc.contributor.departmentDept. of Biologyen_US
dc.identifier.sourcetitleJournal of Cell Scienceen_US
dc.publication.originofpublisherForeignen_US
Appears in Collections:JOURNAL ARTICLES

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.