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A ColE1-type plasmid from Salmonella enteritidis encodes a DNA cytosine methyltransferase

M Ibáñez1, I Alvarez, J M Rodríguez-Peña

  • 1Departamento de Microbiologia II, Facultad de Farmacia, Universidad Complutense, Madrid, Spain.

Gene
|October 10, 1997
PubMed

Insights

The pFM366 plasmid from Salmonella enteritidis contains a DNA methylase. Its activity is regulated by upstream/downstream regions and the rpoS gene, potentially inducing an SOS response in E. coli.

Area of Science:

  • Molecular Biology
  • Microbiology
  • Genetics

Background:

  • The multicopy plasmid pFM366, isolated from Salmonella enteritidis, exhibits DNA methylase activity.
  • This plasmid shares similarities with ColE1-type plasmids and the SsoII restriction-modification system found in Shigella sonnei.

Purpose of the Study:

  • To characterize the genetic organization and functional aspects of the 5.6 kb pFM366 plasmid.
  • To investigate the relationship between pFM366 and other related plasmids, suggesting common evolutionary origins.

Main Methods:

  • Comparative sequence analysis of pFM366 with related plasmids.
  • Functional analysis of the methylase gene, including deletion studies and investigation of regulatory elements.
  • Assessment of the impact of methylase activity on host cell physiology (e.g., growth, SOS response).

Main Results:

  • pFM366 is highly similar to plasmid P4 from Shigella sonnei, encoding a functional cytosine methylase (M. SsoII homolog) and a truncated, inactive restrictase (R. SsoII homolog).
  • Expression of the pFM366 methylase is influenced by flanking DNA regions and negatively regulated by the rpoS gene in E. coli.
  • The methylase activity triggers the SOS response in E. coli, correlating with a delay in bacterial growth.

Conclusions:

  • pFM366 represents a functional DNA methylase system with potential implications for bacterial physiology and evolution.
  • The findings suggest that pFM366 and related plasmids may have arisen from similar recombination events.
  • The induction of the SOS response by pFM366 methylase activity warrants further investigation into its role in bacterial adaptation and virulence.

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