Self-methylation of BspRI DNA-methyltransferase

László Szilák, Csaba Finta, András Patthy, Pál Venetianer, Antal Kiss

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The DNA (cytosine-5)-methyltransferase (m5C-MTase) M.BspRI is able to accept the methyl group from the methyl donor S-adenosyl-L-methionine (AdoMet) in the absence of DNA. Transfer of the methyl group to the enzyme is a slow reaction relative to DNA methylation. Self-methylation is dependent on the native conformation of the enzyme and is inhibited by Sadenosyl- L-homocysteine, DNA and sulfhydryl reagents. Amino acid sequencing of proteolytic peptides obtained from M.BspRI, which had been methylated with [methyl-3H]AdoMet, and thin layer chromatography of the modified amino acid identified two cysteines, Cys156 and Cys181 that bind the methyl group in form of S-methylcysteine. One of the acceptor residues, Cys156 is the highly conserved cysteine which plays the role of the catalytic nucleophile of m5CMTases.

Original languageEnglish
Pages (from-to)2876-2881
Number of pages6
JournalNucleic acids research
Volume22
Issue number15
DOIs
Publication statusPublished - Aug 11 1994

ASJC Scopus subject areas

  • Genetics

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