This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nilsen, T.
Right arrow Articles by Goldberg, M. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nilsen, T.
Right arrow Articles by Goldberg, M. B.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2005, p. 6187-6196, Vol. 187, No. 17
0021-9193/05/$08.00+0     doi:10.1128/JB.187.17.6187-6196.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Presence of Multiple Sites Containing Polar Material in Spherical Escherichia coli Cells That Lack MreB

Trine Nilsen,{dagger} Arthur W. Yan,{ddagger} Gregory Gale, and Marcia B. Goldberg*

Infectious Disease Division, Massachusetts General Hospital, Cambridge, Massachusetts

Received 10 November 2004/ Accepted 15 June 2005

In rod-shaped bacteria, certain proteins are specifically localized to the cell poles. The nature of the positional information that leads to the proper localization of these proteins is unclear. In a screen for factors required for the localization of the Shigella sp. actin assembly protein IcsA to the bacterial pole, a mutant carrying a transposon insertion in mreB displayed altered targeting of IcsA. The phenotype of cells containing a transposon insertion in mreB was indistinguishable from that of cells containing a nonpolar mutation in mreB or that of wild-type cells treated with the MreB inhibitor A22. In cells lacking MreB, a green fluorescent protein (GFP) fusion to a cytoplasmic derivative of IcsA localized to multiple sites. Secreted full-length native IcsA was present in multiple faint patches on the surfaces of these cells in a pattern similar to that seen for the cytoplasmic IcsA-GFP fusion. EpsM, the polar Vibrio cholerae inner membrane protein, also localized to multiple sites in mreB cells and colocalized with IcsA, indicating that localization to multiple sites is not unique to IcsA. Our results are consistent with the requirement, either direct or indirect, for MreB in the restriction of certain polar material to defined sites within the cell and, in the absence of MreB, with the formation of ectopic sites containing polar material.

* Corresponding author. Mailing address: Bacterial Pathogenesis Laboratories, University Park, 65 Landsdowne Street, Cambridge, MA 02139. Phone: (617) 768-8740. Fax: (617) 768-8738. E-mail: mgoldberg1{at}partners.org.

{dagger} Present address: US Genomics, Woburn, MA.

{ddagger} Present address: Tufts Medical School, Boston, MA.

Journal of Bacteriology, September 2005, p. 6187-6196, Vol. 187, No. 17
0021-9193/05/$08.00+0     doi:10.1128/JB.187.17.6187-6196.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Bendezu, F. O., de Boer, P. A. J. (2008). Conditional Lethality, Division Defects, Membrane Involution, and Endocytosis in mre and mrd Shape Mutants of Escherichia coli. J. Bacteriol. 190: 1792-1811 [Abstract] [Full Text]  
  • Srivastava, P., Demarre, G., Karpova, T. S., McNally, J., Chattoraj, D. K. (2007). Changes in Nucleoid Morphology and Origin Localization upon Inhibition or Alteration of the Actin Homolog, MreB, of Vibrio cholerae. J. Bacteriol. 189: 7450-7463 [Abstract] [Full Text]  
  • Robertson, G. T., Doyle, T. B., Du, Q., Duncan, L., Mdluli, K. E., Lynch, A. S. (2007). A Novel Indole Compound That Inhibits Pseudomonas aeruginosa Growth by Targeting MreB Is a Substrate for MexAB-OprM. J. Bacteriol. 189: 6870-6881 [Abstract] [Full Text]  
  • Taghbalout, A., Rothfield, L. (2007). RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton. Proc. Natl. Acad. Sci. USA 104: 1667-1672 [Abstract] [Full Text]  
  • Carballido-Lopez, R. (2006). The Bacterial Actin-Like Cytoskeleton. Microbiol. Mol. Biol. Rev. 70: 888-909 [Abstract] [Full Text]  
  • Pradel, N., Santini, C.-L., Bernadac, A., Fukumori, Y., Wu, L.-F. (2006). Biogenesis of actin-like bacterial cytoskeletal filaments destined for positioning prokaryotic magnetic organelles. Proc. Natl. Acad. Sci. USA 103: 17485-17489 [Abstract] [Full Text]  
  • Shih, Y.-L., Rothfield, L. (2006). The Bacterial Cytoskeleton. Microbiol. Mol. Biol. Rev. 70: 729-754 [Abstract] [Full Text]  
  • Kim, S. Y., Gitai, Z., Kinkhabwala, A., Shapiro, L., Moerner, W. E. (2006). Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus. Proc. Natl. Acad. Sci. USA 103: 10929-10934 [Abstract] [Full Text]  
  • Buddelmeijer, N., Francetic, O., Pugsley, A. P. (2006). Green Fluorescent Chimeras Indicate Nonpolar Localization of Pullulanase Secreton Components PulL and PulM.. J. Bacteriol. 188: 2928-2935 [Abstract] [Full Text]  
  • Esue, O., Wirtz, D., Tseng, Y. (2006). GTPase Activity, Structure, and Mechanical Properties of Filaments Assembled from Bacterial Cytoskeleton Protein MreB. J. Bacteriol. 188: 968-976 [Abstract] [Full Text]  
  • Kruse, T., Blagoev, B., Lobner-Olesen, A., Wachi, M., Sasaki, K., Iwai, N., Mann, M., Gerdes, K. (2006). Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli. Genes Dev. 20: 113-124 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»