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    MinD-dependent conformational changes in MinE required for the Min oscillator to spatially regulate cytokinesis

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    Issue Date
    2011-08-05
    Author
    Park, Kyung-Tae
    Wu, Wei
    Battaile, Kevin P.
    Lovell, Scott
    Holyoak, Todd
    Lutkenhaus, Joe
    Publisher
    Elsevier
    Type
    Article
    Article Version
    Scholarly/refereed, author accepted manuscript
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    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.
    URI
    http://hdl.handle.net/1808/23206
    DOI
    https://doi.org/10.1016/j.cell.2011.06.042
    Collections
    • Higuchi Biosciences Center Scholarly Works [54]
    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.

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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