Present address: Institute of Biological Chemistry, Academica Sinica, 128 Sec. 2, Academia Rd., Nankang, Taipei 115, Taiwan.
Assembly of the MreB-associated cytoskeletal ring of Escherichia coli
Article first published online: 11 FEB 2009
© 2009 The Authors. Journal compilation © 2009 Blackwell Publishing Ltd
Volume 72, Issue 1, pages 170–182, April 2009
How to Cite
Vats, P., Shih, Y.-L. and Rothfield, L. (2009), Assembly of the MreB-associated cytoskeletal ring of Escherichia coli. Molecular Microbiology, 72: 170–182. doi: 10.1111/j.1365-2958.2009.06632.x
- Issue published online: 19 MAR 2009
- Article first published online: 11 FEB 2009
- Accepted 2 February, 2009.
The Escherichia coli actin homologue MreB is part of a helical cytoskeletal structure that winds around the cell between the two poles. It has been shown that MreB redistributes during the cell cycle to form circumferential ring structures that flank the cytokinetic FtsZ ring and appear to be associated with division and segregation of the helical cytoskeleton. We show here that the MreB cytoskeletal ring also contains the MreC, MreD, Pbp2 and RodA proteins. Assembly of MreB, MreC, MreD and Pbp2 into the ring structure required the FtsZ ring but no other known components of the cell division machinery, whereas assembly of RodA into the cytoskeletal ring required one or more additional septasomal components. Strikingly, MreB, MreC, MreD and RodA were each able to independently assemble into the cytoskeletal ring and coiled cytoskeletal structures in the absence of any of the other ring components. This excludes the possibility that one or more of these proteins acts as a scaffold for incorporation of the other proteins into these structures. In contrast, incorporation of Pbp2 required the presence of MreC, which may provide a docking site for Pbp2 entry.