Cloning and structure of the BepI modification methylase

Dagmar Kupper, Jian Guang Zhou, Pal Venetianer, Antal Kiss

Research output: Article

14 Citations (Scopus)

Abstract

The gene coding for a CGCG specific DNA methylase has been cloned in E. coli from Brevibacterium epidermidis. The enzyme, named BepI methylase, is probably the cognate methylase of the FnuDII isoschizomer BepI endonuclease isolated from this strain. The expression of BepI methylase in E. coli is dependent on the orientation of the cloned fragment suggesting that the gene is transcribed from a promoter on the plasmid vector. No BepI endonuclease could be detected in the clones producing BepI methylase. The nucleotide sequence of the BepI methylase gene has been determined, it predicts a protein of 403 amino acids (M: 45, 447). Analysis of the amino acid sequence deduced from the nucleotide sequence revealed similarities between the BepI methylase and other cytosine methylases. M.BepI methylates the external cytosine in its recognition sequence.

Original languageEnglish
Pages (from-to)1077-1088
Number of pages12
JournalNucleic acids research
Volume17
Issue number3
DOIs
Publication statusPublished - febr. 11 1989

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ASJC Scopus subject areas

  • Genetics

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