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. 1995 Aug;39(8):1871-4.
doi: 10.1128/AAC.39.8.1871.

Cloning and characterization of the Pseudomonas aeruginosa pbpB gene encoding penicillin-binding protein 3

X Liao  1 , R E Hancock
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Cloning and characterization of the Pseudomonas aeruginosa pbpB gene encoding penicillin-binding protein 3

X Liao et al. Antimicrob Agents Chemother. 1995 Aug.

Abstract

Clones containing the pbpB gene which encodes penicillin-binding protein (PBP) 3 of Pseudomonas aeruginosa were detected by hybridization by PCR amplification with primers based on the conserved sequences of high-molecular-weight PBPs. The translated amino acid sequence demonstrated 45% identity and had a total of 66% conserved amino acids relative to the Escherichia coli PBP3. The pbpB gene was located upstream of a gene homologous to the E. coli murE gene, which encodes uridine diphosphate-N-acetyl muramic acid-tripeptide synthetase. The overexpressed pbpB gene product reacted with 3H-penicillin G and had an apparent molecular weight of 60,000.

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