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MinD-dependent conformational changes in MinE required for the Min oscillator to spatially regulate cytokinesis
dc.contributor.author | Park, Kyung-Tae | |
dc.contributor.author | Wu, Wei | |
dc.contributor.author | Battaile, Kevin P. | |
dc.contributor.author | Lovell, Scott | |
dc.contributor.author | Holyoak, Todd | |
dc.contributor.author | Lutkenhaus, Joe | |
dc.date.accessioned | 2017-02-20T22:09:37Z | |
dc.date.available | 2017-02-20T22:09:37Z | |
dc.date.issued | 2011-08-05 | |
dc.identifier.citation | Park, 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.uri | http://hdl.handle.net/1808/23206 | |
dc.description.abstract | MinD 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.publisher | Elsevier | en_US |
dc.title | MinD-dependent conformational changes in MinE required for the Min oscillator to spatially regulate cytokinesis | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Lovell, Scott | |
kusw.kudepartment | Higuchi Biosciences Center | en_US |
dc.identifier.doi | 10.1016/j.cell.2011.06.042 | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.rights.accessrights | openAccess |