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Title: The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis.

Abstract

In E. coli, MinD recruits MinE to the membrane, leading to a coupled oscillation required for spatial regulation of the cytokinetic Z ring. How these proteins interact, however, is not clear because the MinD-binding regions of MinE are sequestered within a six-stranded {beta} sheet and masked by N-terminal helices. minE mutations that restore interaction between some MinD and MinE mutants were isolated. These mutations alter the MinE structure leading to release of the MinD-binding regions and the N-terminal helices that bind the membrane. Crystallization of MinD-MinE complexes revealed a four-stranded {beta} sheet MinE dimer with the released {beta} strands (MinD-binding regions) converted to {alpha} helices bound to MinD dimers. These results identify the MinD-dependent conformational changes in MinE that convert it from a latent to an active form and lead to a model of how MinE persists at the MinD-membrane surface.

Authors:
; ; ; ; ;  [1];  [2]
  1. (Kansas)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
1021792
Resource Type:
Journal Article
Journal Name:
Cell
Additional Journal Information:
Journal Volume: 146; Journal Issue: (3) ; 08, 2011; Journal ID: ISSN 0092-8674
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; CONFORMATIONAL CHANGES; CRYSTALLIZATION; DIMERS; MUTANTS; MUTATIONS; OSCILLATIONS; OSCILLATORS; PROTEINS; REGULATIONS

Citation Formats

Park, Kyung-Tase, Wu, Wei, Battaile, Kevin P., Lovell, Scott, Holyoak, Todd, Lutkenhaus, Joe, and HWMRI). The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis.. United States: N. p., 2011. Web. doi:10.1016/j.cell.2011.06.042.
Park, Kyung-Tase, Wu, Wei, Battaile, Kevin P., Lovell, Scott, Holyoak, Todd, Lutkenhaus, Joe, & HWMRI). The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis.. United States. doi:10.1016/j.cell.2011.06.042.
Park, Kyung-Tase, Wu, Wei, Battaile, Kevin P., Lovell, Scott, Holyoak, Todd, Lutkenhaus, Joe, and HWMRI). Fri . "The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis.". United States. doi:10.1016/j.cell.2011.06.042.
@article{osti_1021792,
title = {The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis.},
author = {Park, Kyung-Tase and Wu, Wei and Battaile, Kevin P. and Lovell, Scott and Holyoak, Todd and Lutkenhaus, Joe and HWMRI)},
abstractNote = {In E. coli, MinD recruits MinE to the membrane, leading to a coupled oscillation required for spatial regulation of the cytokinetic Z ring. How these proteins interact, however, is not clear because the MinD-binding regions of MinE are sequestered within a six-stranded {beta} sheet and masked by N-terminal helices. minE mutations that restore interaction between some MinD and MinE mutants were isolated. These mutations alter the MinE structure leading to release of the MinD-binding regions and the N-terminal helices that bind the membrane. Crystallization of MinD-MinE complexes revealed a four-stranded {beta} sheet MinE dimer with the released {beta} strands (MinD-binding regions) converted to {alpha} helices bound to MinD dimers. These results identify the MinD-dependent conformational changes in MinE that convert it from a latent to an active form and lead to a model of how MinE persists at the MinD-membrane surface.},
doi = {10.1016/j.cell.2011.06.042},
journal = {Cell},
issn = {0092-8674},
number = (3) ; 08, 2011,
volume = 146,
place = {United States},
year = {2011},
month = {9}
}