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Journal of Bacteriology, January 2001, p. 200-206, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.200-206.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Differential Responses of Escherichia coli Cells Expressing Cytoplasmic Domain Mutants of Penicillin-Binding Protein 1b after Impairment of Penicillin-Binding Proteins 1a and 3

Christian Chalut,1 Xavier Charpentier,1 Marie-Hélène Remy,1 and Jean-Michel Masson1,2,*

Institut de Pharmacologie et de Biologie Structurale, UMR 5089 du CNRS,1 and Institut National des Sciences Appliquées de Toulouse,2 Toulouse, France

Received 17 July 2000/Accepted 9 October 2000

Penicillin-binding protein 1b (PBP1b) is the major high-molecular-weight PBP in Escherichia coli. Although it is coded by a single gene, it is usually found as a mixture of three isoforms which vary with regard to the length of their N-terminal cytoplasmic tail. We show here that although the cytoplasmic tail seems to play no role in the dimerization of PBP1b, as was originally suspected, only the full-length protein is able to protect the cells against lysis when both PBP1a and PBP3 are inhibited by antibiotics. This suggests a specific role for the full-length PBP1b in the multienzyme peptidoglycan-synthesizing complex that cannot be fulfilled by either PBP1a or the shorter PBP1b proteins. Moreover, we have shown by alanine-stretch-scanning mutagenesis that (i) residues R11 to G13 are major determinants for correct translocation and folding of PBP1b and that (ii) the specific interactions involving the full-length PBP1b can be ascribed to the first six residues at the N-terminal end of the cytoplasmic domain. These results are discussed in terms of the interactions with other components of the murein-synthesizing complex.

* Corresponding author. Mailing address: IPBS-CNRS, 205, route de Narbonne, 31077 Toulouse Cedex, France. Phone: (33) 0561-17-54-76. Fax: (33) 0561-17-59-94. E-mail: masson{at}ipbs.fr.

Journal of Bacteriology, January 2001, p. 200-206, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.200-206.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Meisel, U., Holtje, J.-V., Vollmer, W. (2003). Overproduction of Inactive Variants of the Murein Synthase PBP1B Causes Lysis in Escherichia coli. J. Bacteriol. 185: 5342-5348 [Abstract] [Full Text]  
  • Goffin, C., Ghuysen, J.-M. (2002). Biochemistry and Comparative Genomics of SxxK Superfamily Acyltransferases Offer a Clue to the Mycobacterial Paradox: Presence of Penicillin-Susceptible Target Proteins versus Lack of Efficiency of Penicillin as Therapeutic Agent. Microbiol. Mol. Biol. Rev. 66: 702-738 [Abstract] [Full Text]  
  • Charpentier, X., Chalut, C., Remy, M.-H., Masson, J.-M. (2002). Penicillin-Binding Proteins 1a and 1b Form Independent Dimers in Escherichia coli. J. Bacteriol. 184: 3749-3752 [Abstract] [Full Text]  


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