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Journal of Bacteriology, January 2005, p. 54-64, Vol. 187, No. 1
0021-9193/05/$08.00+0     doi:10.1128/JB.187.1.54-64.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Localization of MreB in Rhodobacter sphaeroides under Conditions Causing Changes in Cell Shape and Membrane Structure{dagger}

Peter M. Slovak, George H. Wadhams, and Judith P. Armitage*

Department of Biochemistry, University of Oxford, Oxford, United Kingdom

Received 7 April 2004/ Accepted 1 June 2004

MreB is thought to be a bacterial actin homolog that defines the morphology of rod-shaped bacteria. Rhodobacter sphaeroides changes shape, from a rod to coccobacillus, and undergoes extensive cytoplasmic membrane invagination when it switches from aerobic to photoheterotrophic growth. The role of MreB in defining R. sphaeroides shape was therefore investigated. Attempts at deleting or insertionally inactivating mreB were unsuccessful under all growth conditions. Immunofluorescence microscopy showed MreB localized to mid-cell in elongating cells under both aerobic and photoheterotrophic conditions. Three-dimensional reconstruction showed that MreB formed a ring at mid-cell. MreB remained at mid-cell as septation began but localized to new sites in the daughter cells before the completion of septation. MreB localized to putative septation sites in cephalexin-treated filamentous cells. Genomic single-copy mreB was replaced with gfp-mreB, and green fluorescent protein (GFP)-MreB localized in the same pattern, as seen with immunofluorescence microscopy. Some of the cells expressing GFP-MreB were abnormal, principally displaying an increase in cell width, suggesting that the fusion was not fully functional in all cells. GFP-MreB localized to swellings at mid-cell in cells treated with the penicillin-binding protein 2 inhibitor amdinocillin. These data suggest that MreB is essential in R. sphaeroides, performing a role at mid-cell in elongating cells, and in early septation, putatively in the cytoplasmic control of the peptidoglycan synthetic complexes.

* Corresponding author. Mailing address: Department of Biochemistry, University of Oxford, South Parks Rd., Oxford, OX1 3QU United Kingdom. Phone: (44) 186 527 5299. Fax: (44) 186 527 5297. E-mail: armitage{at}bioch.ox.ac.uk.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/

Journal of Bacteriology, January 2005, p. 54-64, Vol. 187, No. 1
0021-9193/05/$08.00+0     doi:10.1128/JB.187.1.54-64.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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