Assembly properties of the Bacillus subtilis actin, MreB
Article first published online: 30 DEC 2008
Copyright © 2008 Wiley-Liss, Inc.
Cell Motility and the Cytoskeleton
Volume 66, Issue 2, pages 109–118, February 2009
How to Cite
Mayer, J. A. and Amann, K. J. (2009), Assembly properties of the Bacillus subtilis actin, MreB. Cell Motil. Cytoskeleton, 66: 109–118. doi: 10.1002/cm.20332
- Issue published online: 16 JAN 2009
- Article first published online: 30 DEC 2008
- Manuscript Accepted: 1 DEC 2008
- Manuscript Received: 12 AUG 2008
- American Heart Association Scientist Development. Grant Number: 0430162N
- Bacillus subtilis;
The bacterial actin MreB has been implicated in a variety of cellular roles including cell shape determination, cell wall synthesis, chromosome condensation and segregation, and the establishment and maintenance of cell polarity. Toward elucidating a clearer understanding of how MreB functions inside the bacterial cell, we investigated biochemically the polymerization of MreB from Bacillus subtilis. Light scattering and sedimentation assays revealed pH-, ionic-, cationic-, and temperature-dependent behavior. B. subtilis MreB polymerizes in the presence of millimolar divalent cations in a protein concentration-dependent manner. Polymerization is favored by decreasing pH and inhibited by monovalent salts and low temperatures. Although B. subtilis MreB binds and hydrolyzes both ATP and GTP, it does not require a bound nucleotide for assembly and polymerizes indistinguishably regardless of the nucleotide species bound, with a critical concentration of ∼900 nM. A number of the presently reported properties of B. subtilis MreB differ significantly from those of T. maritima MreB1 (Bean and Amann : Biochemistry 47: 826–835), including the nucleotide requirements and temperature and ionic effects on polymerization state. These observations collectively suggest that additional factors interact with MreB to account for its complex dynamic behavior in cells. Cell Motil. Cytoskeleton 2009. © 2008 Wiley-Liss, Inc.