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Nucleic Acids Research, 1989, Vol. 17, No. 3 1077-1088
© 1989

ENZYMOLOGY

Cloning and structure of the BepI modification methylase

Dagmar Kupper*, Jian-Guang Zhou*, Pal Venetianer and Antal Kiss

Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences PO Box 521, 6701 Szeged, Hungary

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.

*Present addresses: Biotechnology Centre, Martin Luther University, Universitatsring 5, Halle 4020, GDR and +Molecular Genetics Centre, PO Box 130 (8), Beijing 100850, China


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