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Journal of Bacteriology, February 2000, p. 1074-1079, Vol. 182, No. 4
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Cloning, Characterization, and Inactivation of the Gene pbpC, Encoding Penicillin-Binding Protein 3 of Staphylococcus aureus

Mariana G. Pinho,1,2 Hermínia de Lencastre,1,2 and Alexander Tomasz1,*

Laboratory of Microbiology, The Rockefeller University, New York, New York 10021,1 and Molecular Genetics Unit, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal2

Received 22 September 1999/Accepted 18 November 1999

The gene pbpC from Staphylococcus aureus was sequenced: it encodes a 691-amino-acid protein with all of the conserved motifs of a class B high-molecular-weight penicillin-binding protein (PBP), including the transpeptidase conserved motifs SXXK, SXN, and KTG. Insertional inactivation of pbpC and introduction of the intact gene in a laboratory mutant missing PBP 3 showed that the pbpC gene encodes the staphylococcal PBP 3. Inactivation of pbpC caused no detectable change in the muropeptide composition of cell wall peptidoglycan and had only minimum, if any, effect on growth rates, but caused a small but significant decrease in rates of autolysis. Cells of abnormal size and shape and disoriented septa were produced when bacteria with inactivated pbpC were grown in the presence of a sub-MIC of methicillin.

* Corresponding author. Mailing address: Laboratory of Microbiology, The Rockefeller University, 1230 York Ave., New York, NY 10021. Phone: (212) 327-8278. Fax: (212) 327-8688. E-mail: tomasz{at}rockvax.rockefeller.edu.

Journal of Bacteriology, February 2000, p. 1074-1079, Vol. 182, No. 4
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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