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Identification of mucAB-like homologs on two IncT plasmids, R394 and Rts-1

W H Koch1, A R Fernández de Henestrosa, R Woodgate

  • 1Molecular Biology Branch, Food and Drug Administration, 20204, Washington, DC, USA.

Mutation Research
|December 7, 2000
PubMed

Insights

Researchers developed a new assay to identify umuC-like genes in bacteria. This method identified mucAB-like operons on plasmids, revealing inactive MucB proteins but also potential new DNA polymerases.

Area of Science:

  • Molecular Biology
  • Genetics
  • Microbiology

Background:

  • Lesion-replicating DNA polymerases are crucial for DNA repair and mutagenesis.
  • The UmuC-like subfamily of these polymerases can be further classified into five groups, including MucAB.
  • Some UmuC-like genes are inactive in their native state but can enhance mutagenesis when overexpressed.

Purpose of the Study:

  • To develop a functional assay for identifying umuC-like genes in situ.
  • To investigate the presence and activity of umuC-like genes on bacterial plasmids R394 and Rts-1.

Main Methods:

  • Phylogenetic analysis to classify DNA polymerases.
  • Design of degenerate primers targeting conserved regions of UmuC-like polymerases.
  • DNA sequencing of plasmid regions and analysis of gene expression.
  • Complementation assays using an Escherichia coli strain deficient in umuDC genes.

Main Results:

  • Degenerate primers successfully identified mucAB-like operons on IncT plasmids R394 and Rts-1.
  • Sequence analysis revealed LexA-regulated genes similar to E. coli tus and impC adjacent to mucAB((R394)).
  • Both R394 and Rts-1 mucB genes contained insertions leading to truncated, inactive MucB proteins.
  • Plasmid R394 did not restore mutagenesis, but Rts-1 significantly increased MMS-induced SOS mutagenesis.

Conclusions:

  • The developed assay is effective for identifying umuC-like genes in situ.
  • The Rts-1 plasmid may encode an uncharacterized umu-like DNA polymerase responsible for enhanced mutagenesis.
  • Further investigation is needed to identify the novel umu-like homolog on the Rts-1 plasmid.

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