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Journal of Bacteriology, May 2006, p. 3516-3524, Vol. 188, No. 10
0021-9193/06/$08.00+0     doi:10.1128/JB.188.10.3516-3524.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Direct Visualization of Red Fluorescent Lipoproteins Indicates Conservation of the Membrane Sorting Rules in the Family Enterobacteriaceae

Shawn Lewenza, Dominique Vidal-Ingigliardi, and Anthony P. Pugsley*

Molecular Genetics Unit and CNRS URA2172, Institut Pasteur, 75724 Paris, France

Received 2 February 2006/ Accepted 9 March 2006

Chimeras created by fusing the monomeric red fluorescent protein (RFP) to a bacterial lipoprotein signal peptide (lipoRFPs) were visualized in the cell envelope by epifluorescence microscopy. Plasmolysis of the bacteria separated the inner and outer membranes, allowing the specific subcellular localization of lipoRFPs to be determined in situ. When equipped with the canonical inner membrane lipoprotein retention signal CDSR, lipoRFP was located in the inner membrane in Escherichia coli, whereas the outer membrane sorting signal CSSR caused lipoRFP to localize to the outer membrane. CFSR-RFP was also routed to the outer membrane, but CFNSR-RFP was located in the inner membrane, consistent with previous data showing that this sequence functions as an inner membrane retention signal. These four lipoproteins exhibited identical localization patterns in a panel of members of the family Enterobacteriaceae, showing that the lipoprotein sorting rules are conserved in these bacteria and validating the use of E. coli as a model system. Although most predicted inner membrane lipoproteins in these bacteria have an aspartate residue after the fatty acylated N-terminal cysteine residue, alternative signals such as CFN can and probably do function in parallel, as indicated by the existence of putative inner membrane lipoproteins with this sequence at their N termini.

* Corresponding author. Mailing address: Molecular Genetics Unit, Institut Pasteur, 25, rue du Dr. Roux, 75724 Paris CEDEX 15, France. Phone: 33/0-145688494. Fax: 33/0-145688960. E-mail: max{at}pasteur.fr.

Journal of Bacteriology, May 2006, p. 3516-3524, Vol. 188, No. 10
0021-9193/06/$08.00+0     doi:10.1128/JB.188.10.3516-3524.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • 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]  
  • Vidal-Ingigliardi, D., Lewenza, S., Buddelmeijer, N. (2007). Identification of Essential Residues in Apolipoprotein N-Acyl Transferase, a Member of the CN Hydrolase Family. J. Bacteriol. 189: 4456-4464 [Abstract] [Full Text]  
  • Narita, S.-i., Tokuda, H. (2007). Amino Acids at Positions 3 and 4 Determine the Membrane Specificity of Pseudomonas aeruginosa Lipoproteins. J. Biol. Chem. 282: 13372-13378 [Abstract] [Full Text]  
  • Francetic, O., Buddelmeijer, N., Lewenza, S., Kumamoto, C. A., Pugsley, A. P. (2007). Signal Recognition Particle-Dependent Inner Membrane Targeting of the PulG Pseudopilin Component of a Type II Secretion System. J. Bacteriol. 189: 1783-1793 [Abstract] [Full Text]  


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