A murC gene in Porphyromonas gingivalis 381

Microbiology (Reading). 1995 Sep;141 ( Pt 9):2047-52. doi: 10.1099/13500872-141-9-2047.

Abstract

The gene encoding a 51 kDa polypeptide of Porphyromonas gingivalis 381 was isolated by immunoblotting using an antiserum raised against P. gingivalis alkaline phosphatase. DNA sequence analysis of a 2.5 kb DNA fragment containing a gene encoding the 51 kDa protein revealed one complete and two incomplete ORFs. Database searches using the FASTA program revealed significant homology between the P. gingivalis 51 kDa protein and the MurC protein of Escherichia coli, which functions in peptidoglycan synthesis. The cloned 51 kDa protein encoded a functional product that complemented an E. coli murC mutant. Moreover, the ORF just upstream of murC coded for a protein that was 31% homologous with the E. coli MurG protein. The ORF just downstream of murC coded for a protein that was 17% homologous with the Streptococcus pneumoniae penicillin-binding protein 2B (PBP2B), which functions in peptidoglycan synthesis and is responsible for antibiotic resistance. These results suggest that P. gingivalis contains a homologue of the E. coli peptidoglycan synthesis gene murC and indicate the possibility of a cluster of genes responsible for cell division and cell growth, as in the E. coli mra region.

Publication types

  • Comparative Study

MeSH terms

  • Alkaline Phosphatase / genetics
  • Amino Acid Sequence
  • Aminoacyltransferases*
  • Bacterial Outer Membrane Proteins*
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / isolation & purification
  • Base Sequence
  • Carrier Proteins / genetics*
  • Carrier Proteins / isolation & purification
  • Cell Division / genetics
  • Cloning, Molecular
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Genes, Bacterial*
  • Genetic Complementation Test
  • Hexosyltransferases*
  • Molecular Sequence Data
  • Muramoylpentapeptide Carboxypeptidase / genetics*
  • Muramoylpentapeptide Carboxypeptidase / isolation & purification
  • N-Acetylglucosaminyltransferases / genetics
  • Open Reading Frames
  • Penicillin Resistance / genetics
  • Penicillin-Binding Proteins
  • Peptide Synthases / genetics*
  • Peptidoglycan / biosynthesis
  • Peptidyl Transferases*
  • Porphyromonas gingivalis / enzymology
  • Porphyromonas gingivalis / genetics*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Species Specificity
  • Streptococcus pneumoniae / genetics

Substances

  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Carrier Proteins
  • Penicillin-Binding Proteins
  • Peptidoglycan
  • Aminoacyltransferases
  • penicillin-binding protein 2b, Streptococcus
  • Peptidyl Transferases
  • Hexosyltransferases
  • N-Acetylglucosaminyltransferases
  • UDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
  • Alkaline Phosphatase
  • Muramoylpentapeptide Carboxypeptidase
  • Peptide Synthases
  • UDP-N-acetylmuramoyl-alanine synthetase

Associated data

  • GENBANK/D84504