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Journal of Bacteriology, June 1999, p. 3852-3856, Vol. 181, No. 12
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Mutational Analysis of the Streptococcus pneumoniae Bimodular Class A Penicillin-Binding Proteins

Johanna Paik,1 Iza Kern,1,dagger Rudi Lurz,1 and Regine Hakenbeck2,*

Department of Microbiology, University of Kaiserslautern, D-67663 Kaiserslautern,2 and Max-Planck Institut für Molekulare Genetik, D-14185 Berlin,1 Germany

Received 15 January 1999/Accepted 17 March 1999

One group of penicillin target enzymes, the class A high-molecular-weight penicillin-binding proteins (PBPs), are bimodular enzymes. In addition to a central penicillin-binding-transpeptidase domain, they contain an N-terminal putative glycosyltransferase domain. Mutations in the genes for each of the three Streptococcus pneumoniae class A PBPs, PBP1a, PBP1b, and PBP2a, were isolated by insertion duplication mutagenesis within the glycosyltransferase domain, documenting that their function is not essential for cellular growth in the laboratory. PBP1b PBP2a and PBP1a PBP1b double mutants could also be isolated, and both showed defects in positioning of the septum. Attempts to obtain a PBP2a PBP1a double mutant failed. All mutants with a disrupted pbp2a gene showed higher sensitivity to moenomycin, an antibiotic known to inhibit PBP-associated glycosyltransferase activity, indicating that PBP2a is the primary target for glycosyltransferase inhibitors in S. pneumoniae.

* Corresponding author. Mailing address: Department of Microbiology, University of Kaiserslautern, Paul-Ehrlich Straße, D-67663 Kaiserslautern, Germany. Phone: 49-631-205-2353. Fax: 49-631-205-3799. E-mail: hakenb{at}rhrk.uni-kl.de.

dagger Present address: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warsaw, Poland.

Journal of Bacteriology, June 1999, p. 3852-3856, Vol. 181, No. 12
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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