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Journal of Bacteriology, May 1999, p. 2970-2972, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Disulfide Bridges Are Not Involved in Penicillin-Binding Protein 1b Dimerization in Escherichia coli

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

Institut de Pharmacologie et de Biologie Structurale du CNRS1 and Institut National des Sciences Appliquées de Toulouse,2 Toulouse, France

Received 8 December 1998/Accepted 24 February 1999

PBP1b can be found as a dimer in Escherichia coli. Previous results suggested that dimerization involved the cysteine(s) in an intermolecular disulfide bond. We show that either deletion mutants or a mutant without cysteines is fully active and still binds penicillin and that the latter can also form dimers.

* 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, May 1999, p. 2970-2972, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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