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 Ghosh, A. S.
Right arrow Articles by Young, K. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ghosh, A. S.
Right arrow Articles by Young, K. D.

 Previous Article  |  Next Article 

Journal of Bacteriology, March 2005, p. 1913-1922, Vol. 187, No. 6
0021-9193/05/$08.00+0     doi:10.1128/JB.187.6.1913-1922.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Helical Disposition of Proteins and Lipopolysaccharide in the Outer Membrane of Escherichia coli

Anindya S. Ghosh{dagger} and Kevin D. Young*

Department of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, North Dakota

Received 22 October 2004/ Accepted 3 December 2004

In bacteria, several physiological processes once thought to be the products of uniformly dispersed reactions are now known to be highly asymmetric, with some exhibiting interesting geometric localizations. In particular, the cell envelope of Escherichia coli displays a form of subcellular differentiation in which peptidoglycan and outer membrane proteins at the cell poles remain stable for generations while material in the lateral walls is diluted by growth and turnover. To determine if material in the side walls was organized in any way, we labeled outer membrane proteins with succinimidyl ester-linked fluorescent dyes and then grew the stained cells in the absence of dye. Labeled proteins were not evenly dispersed in the envelope but instead appeared as helical ribbons that wrapped around the outside of the cell. By staining the O8 surface antigen of E. coli 2443 with a fluorescent derivative of concanavalin A, we observed a similar helical organization for the lipopolysaccharide (LPS) component of the outer membrane. Fluorescence recovery after photobleaching indicated that some of the outer membrane proteins remained freely diffusible in the side walls and could also diffuse into polar domains. On the other hand, the LPS O antigen was virtually immobile. Thus, the outer membrane of E. coli has a defined in vivo organization in which a subfraction of proteins and LPS are embedded in stable domains at the poles and along one or more helical ribbons that span the length of this gram-negative rod.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58202-9037. Phone: (701) 777-2624. Fax: (701) 777-2054. E-mail: kyoung{at}medicine.nodak.edu.

{dagger} Present address: Department of Biotechnology, Indian Institute of Technology, Kharagpur 721302, West Bengal, India.

Journal of Bacteriology, March 2005, p. 1913-1922, Vol. 187, No. 6
0021-9193/05/$08.00+0     doi:10.1128/JB.187.6.1913-1922.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Valencia-Burton, M., Shah, A., Sutin, J., Borogovac, A., McCullough, R. M., Cantor, C. R., Meller, A., Broude, N. E. (2009). Spatiotemporal patterns and transcription kinetics of induced RNA in single bacterial cells. Proc. Natl. Acad. Sci. USA 106: 16399-16404 [Abstract] [Full Text]  
  • Mileykovskaya, E., Ryan, A. C., Mo, X., Lin, C.-C., Khalaf, K. I., Dowhan, W., Garrett, T. A. (2009). Phosphatidic Acid and N-Acylphosphatidylethanolamine Form Membrane Domains in Escherichia coli Mutant Lacking Cardiolipin and Phosphatidylglycerol. J. Biol. Chem. 284: 2990-3000 [Abstract] [Full Text]  
  • Buddelmeijer, N., Krehenbrink, M., Pecorari, F., Pugsley, A. P. (2009). Type II Secretion System Secretin PulD Localizes in Clusters in the Escherichia coli Outer Membrane. J. Bacteriol. 191: 161-168 [Abstract] [Full Text]  
  • Lewenza, S., Mhlanga, M. M., Pugsley, A. P. (2008). Novel Inner Membrane Retention Signals in Pseudomonas aeruginosa Lipoproteins. J. Bacteriol. 190: 6119-6125 [Abstract] [Full Text]  
  • Tran, A. X., Trent, M. S., Whitfield, C. (2008). The LptA Protein of Escherichia coli Is a Periplasmic Lipid A-binding Protein Involved in the Lipopolysaccharide Export Pathway. J. Biol. Chem. 283: 20342-20349 [Abstract] [Full Text]  
  • Jose, J., Meyer, T. F. (2007). The Autodisplay Story, from Discovery to Biotechnical and Biomedical Applications. Microbiol. Mol. Biol. Rev. 71: 600-619 [Abstract] [Full Text]  
  • Varma, A., de Pedro, M. A., Young, K. D. (2007). FtsZ Directs a Second Mode of Peptidoglycan Synthesis in Escherichia coli. J. Bacteriol. 189: 5692-5704 [Abstract] [Full Text]  
  • Priyadarshini, R., de Pedro, M. A., Young, K. D. (2007). Role of Peptidoglycan Amidases in the Development and Morphology of the Division Septum in Escherichia coli. J. Bacteriol. 189: 5334-5347 [Abstract] [Full Text]  
  • Geissler, B., Shiomi, D., Margolin, W. (2007). The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring. Microbiology 153: 814-825 [Abstract] [Full Text]  
  • Young, K. D. (2006). The Selective Value of Bacterial Shape. Microbiol. Mol. Biol. Rev. 70: 660-703 [Abstract] [Full Text]  
  • Shih, Y.-L., Rothfield, L. (2006). The Bacterial Cytoskeleton. Microbiol. Mol. Biol. Rev. 70: 729-754 [Abstract] [Full Text]  
  • Wagner, J. K., Setayeshgar, S., Sharon, L. A., Reilly, J. P., Brun, Y. V. (2006). From the Cover: A nutrient uptake role for bacterial cell envelope extensions. Proc. Natl. Acad. Sci. USA 103: 11772-11777 [Abstract] [Full Text]  
  • McAdams, H. H. (2006). Bacterial stalks are nutrient-scavenging antennas. Proc. Natl. Acad. Sci. USA 103: 11435-11436 [Full Text]  
  • Jain, S., van Ulsen, P., Benz, I., Schmidt, M. A., Fernandez, R., Tommassen, J., Goldberg, M. B. (2006). Polar Localization of the Autotransporter Family of Large Bacterial Virulence Proteins. J. Bacteriol. 188: 4841-4850 [Abstract] [Full Text]  
  • Lewenza, S., Vidal-Ingigliardi, D., Pugsley, A. P. (2006). Direct visualization of red fluorescent lipoproteins indicates conservation of the membrane sorting rules in the family enterobacteriaceae.. J. Bacteriol. 188: 3516-3524 [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]  
  • Dye, N. A., Pincus, Z., Theriot, J. A., Shapiro, L., Gitai, Z. (2005). Two independent spiral structures control cell shape in Caulobacter. Proc. Natl. Acad. Sci. USA 102: 18608-18613 [Abstract] [Full Text]  
  • Divakaruni, A. V., Loo, R. R. O., Xie, Y., Loo, J. A., Gober, J. W. (2005). The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus. Proc. Natl. Acad. Sci. USA 102: 18602-18607 [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»