DNA modification by methyltransferases

Cheng, X. (February 1995) DNA modification by methyltransferases. Curr Opin Struct Biol, 5 (1). pp. 4-10. ISSN 0959-440X (Print)

URL: http://www.ncbi.nlm.nih.gov/pubmed/7773746
DOI: 10.1016/0959-440X(95)80003-J


Enzymatic methylation of DNA plays important roles in both prokaryotes and eukaryotes. Structural study of the HhaI DNA methyltransferase has provided considerable insight into the chemistry of C5-cytosine methylation. The DNA-protein complex reveals a substrate cytosine flipped out of the double helix during the reaction, and a novel two-loop DNA-binding motif used for both sequence recognition and flipping the base. Structural comparison of HhaI C5-cytosine methyltransferase, TaqI N6-adenine methyltransferase, and catechol O-methyltransferase reveals a common catalytic domain structure, which might be universal among S-adenosyl-L-methionine (SAM)-dependent methyltransferases.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Animals DNA/ chemistry/ metabolism Humans Methyltransferases/chemistry/ pharmacology Molecular Sequence Data Nucleic Acid Conformation/ drug effects Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.
Subjects: bioinformatics > genomics and proteomics > design > amino acid design
organism description > animal
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase
CSHL Authors:
Communities: CSHL labs
Depositing User: Jessica Koos
Date: February 1995
Date Deposited: 15 Aug 2014 19:13
Last Modified: 15 Aug 2014 19:13
Related URLs:
URI: https://repository.cshl.edu/id/eprint/30573

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