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 Suzuki, M.
Right arrow Articles by Matsumoto, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Suzuki, M.
Right arrow Articles by Matsumoto, K.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2002, p. 5418-5425, Vol. 184, No. 19
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.19.5418-5425.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Envelope Disorder of Escherichia coli Cells Lacking Phosphatidylglycerol

Motoo Suzuki, Hiroshi Hara, and Kouji Matsumoto*

Department of Biochemistry and Molecular Biology, Faculty of Science, Saitama University, Saitama 338-8570, Japan

Received 3 June 2002/ Accepted 9 July 2002

Phosphatidylglycerol, the most abundant acidic phospholipid in Escherichia coli, is considered to play specific roles in various cellular processes that are essential for cell viability. A null mutation of pgsA, which encodes phosphatidylglycerophosphate synthase, does indeed confer lethality. However, pgsA null mutants are viable if they lack the major outer membrane lipoprotein (Lpp) (lpp mutant) (S. Kikuchi, I. Shibuya, and K. Matsumoto, J. Bacteriol. 182:371-376, 2000). Here we show that Lpp expressed from a plasmid causes cell lysis in a pgsA lpp double mutant. The envelopes of cells harvested just before lysis could not be separated into outer and inner membrane fractions by sucrose density gradient centrifugation. In contrast, expression of a mutant Lpp (Lpp{Delta}K) lacking the COOH-terminal lysine residue (required for covalent linking to peptidoglycan) did not cause lysis and allowed for the clear separation of the outer and inner membranes. We propose that in pgsA mutants Lpp{Delta}K could not be modified by the addition of a diacylglyceryl moiety normally provided by phosphatidylglycerol and that this defect caused unmodified Lpp{Delta}K to accumulate in the inner membrane. Although Lpp{Delta}K accumulation did not lead to lysis, the accumulation of unmodified wild-type Lpp apparently led to the covalent linking to peptidoglycan, causing the inner membrane to be anomalously anchored to peptidoglycan and eventually leading to lysis. We suggest that this anomalous anchoring largely explains a major portion of the nonviable phenotypes of pgsA null mutants.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Faculty of Science, Saitama University, 255 Shimo-ohkubo, Saitama, Saitama 338-8570, Japan. Phone: 81-48-858-3406. Fax: 81-48-858-3698. E-mail: koumatsu{at}molbiol.saitama-u.ac.jp.

Journal of Bacteriology, October 2002, p. 5418-5425, Vol. 184, No. 19
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.19.5418-5425.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • 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]  
  • Haugen, B. J., Pellett, S., Redford, P., Hamilton, H. L., Roesch, P. L., Welch, R. A. (2007). In Vivo Gene Expression Analysis Identifies Genes Required for Enhanced Colonization of the Mouse Urinary Tract by Uropathogenic Escherichia coli Strain CFT073 dsdA. Infect. Immun. 75: 278-289 [Abstract] [Full Text]  
  • Reva, O. N., Weinel, C., Weinel, M., Bohm, K., Stjepandic, D., Hoheisel, J. D., Tummler, B. (2006). Functional Genomics of Stress Response in Pseudomonas putida KT2440. J. Bacteriol. 188: 4079-4092 [Abstract] [Full Text]  
  • Robichon, C., Vidal-Ingigliardi, D., Pugsley, A. P. (2005). Depletion of Apolipoprotein N-Acyltransferase Causes Mislocalization of Outer Membrane Lipoproteins in Escherichia coli. J. Biol. Chem. 280: 974-983 [Abstract] [Full Text]  
  • Zientz, E., Dandekar, T., Gross, R. (2004). Metabolic Interdependence of Obligate Intracellular Bacteria and Their Insect Hosts. Microbiol. Mol. Biol. Rev. 68: 745-770 [Abstract] [Full Text]  
  • Shiba, Y., Yokoyama, Y., Aono, Y., Kiuchi, T., Kusaka, J., Matsumoto, K., Hara, H. (2004). Activation of the Rcs Signal Transduction System Is Responsible for the Thermosensitive Growth Defect of an Escherichia coli Mutant Lacking Phosphatidylglycerol and Cardiolipin. J. Bacteriol. 186: 6526-6535 [Abstract] [Full Text]  
  • Kawai, F., Shoda, M., Harashima, R., Sadaie, Y., Hara, H., Matsumoto, K. (2004). Cardiolipin Domains in Bacillus subtilis Marburg Membranes. J. Bacteriol. 186: 1475-1483 [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»