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The bacterial actin MreB rotates, and rotation depends on cell-wall assembly.

Authors :
van Teeffelena, Sven
Siyuan Wang
Furchtgott, Leon
Huangd, Kerwyn Casey
Ned S. Wingreen
Joshua W. Shaevitz
Gitai, Zemer
Source :
Proceedings of the National Academy of Sciences of the United States of America; 9/20/2011, Vol. 108 Issue 38, p15822-15827, 6p
Publication Year :
2011

Abstract

Bacterial cells possess multiple cytoskeletal proteins involved in a wide range of cellular processes. These cytoskeletal proteins are dynamic, but the driving forces and cellular functions of these dynamics remain poorly understood. Eukaryotic cytoskeletal dynamics are often driven by motor proteins, but in bacteria no motors that drive cytoskeletal motion have been identified to date. Here, we quantitatively study the dynamics of the Escherichia coli actin homolog MreB, which is essential for the maintenance of rod-like cell shape in bacteria. We find that MreB rotates around the long axis of the cell in a persistent manner. Whereas previous studies have suggested that MreB dynamics are driven by its own polymerization, we show that MreB rotation does not depend on its own polymerization but rather requires the assembly of the peptidoglycan cell wall. The cell-wall synthesis machinery thus either constitutes a novel type of extracellular motor that exerts force on cytoplasmic MreB, or is indirectly required for an as-yetunidentified motor. Biophysical simulations suggest that one function of MreB rotation is to ensure a uniform distribution of new peptidoglycan insertion sites, a necessary condition to maintain rod shape during growth. These findings both broaden the view of cytoskeletal motors and deepen our understanding of the physical basis of bacterial morphogenesis. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00278424
Volume :
108
Issue :
38
Database :
Complementary Index
Journal :
Proceedings of the National Academy of Sciences of the United States of America
Publication Type :
Academic Journal
Accession number :
66701971
Full Text :
https://doi.org/10.1073/pnas.1108999108