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dc.contributor.authorPark, Kyung-Tae
dc.contributor.authorWu, Wei
dc.contributor.authorBattaile, Kevin P.
dc.contributor.authorLovell, Scott
dc.contributor.authorHolyoak, Todd
dc.contributor.authorLutkenhaus, Joe
dc.date.accessioned2017-02-20T22:09:37Z
dc.date.available2017-02-20T22:09:37Z
dc.date.issued2011-08-05
dc.identifier.citationPark, Kyung-Tae, Wei Wu, Kevin P. Battaile, Scott Lovell, Todd Holyoak, and Joe Lutkenhaus. "The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis." Cell 146.3 (2011): 396-407.en_US
dc.identifier.urihttp://hdl.handle.net/1808/23206
dc.description.abstractMinD recruits MinE to the membrane leading to a coupled oscillation required for spatial regulation of the cytokinetic Z ring in E. coli. How these proteins interact, however, is not clear since the MinD binding regions of MinE are sequestered within a 6-stranded β-sheet and masked by N-terminal helices. Here, minE mutations are isolated that restore interaction to some MinD and MinE mutants. These mutations alter the MinE structure releasing the MinD binding regions and N-terminal helices that bind MinD and the membrane, respectively. Crystallization of MinD-MinE complexes reveals a 4-stranded β-sheet MinE dimer with the released β strands (MinD binding regions) converted to α-helices bound to MinD dimers. These results suggest a 6 stranded, β-sheet dimer of MinE ‘senses’ MinD and switches to a 4-stranded β-sheet dimer that binds MinD and contributes to membrane binding. Also, the results indicate how MinE persists at the MinD-membrane surface.en_US
dc.publisherElsevieren_US
dc.titleMinD-dependent conformational changes in MinE required for the Min oscillator to spatially regulate cytokinesisen_US
dc.typeArticleen_US
kusw.kuauthorLovell, Scott
kusw.kudepartmentHiguchi Biosciences Centeren_US
dc.identifier.doi10.1016/j.cell.2011.06.042en_US
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.rights.accessrightsopenAccess


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