Skip Navigation

This Article
Right arrow Print PDF (2349K)
Right arrow An erratum has been published
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Szilák, L.
Right arrow Articles by Kiss, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Szilák, L.
Right arrow Articles by Kiss, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1994, Vol. 22, No. 15 2876-2881
© 1994

MOLECULAR BIOLOGY

Self-methylation of BspRI DNA-methyltransferase

László Szilák, Csaba Finta, András Patthy1, Pál Venetianer and Antal Kiss*

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

*To whom correspondence should be addressed

Received July 15, 1994. Accepted July 1, 1994.

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.

1Agricultural Biotechnology Center, PO Box 170, Gödöllö 2101, Hungary


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Protein Sci.Home page
V. N. Lapko, D. L. Smith, and J. B. Smith
Methylation and carbamylation of human {gamma}-crystallins
Protein Sci., August 1, 2003; 12(8): 1762 - 1774.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. K. Bhattacharya and A. K. Dubey
Kinetic Mechanism of Cytosine DNA Methyltransferase MspI
J. Biol. Chem., May 21, 1999; 274(21): 14743 - 14749.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. V. R. Reddy and D. N. Rao
Probing the Role of Cysteine Residues in the EcoP15I DNA Methyltransferase
J. Biol. Chem., September 11, 1998; 273(37): 23866 - 23876.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.