DNA modification by methyltransferases.

X Cheng

doi:10.1016/0959-440x(95)80003-j

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DNA modification by methyltransferases.

X Cheng

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Abstract

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.

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Amino Acid Sequence Animals DNA Humans Methyltransferases Molecular Sequence Data Nucleic Acid Conformation Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.Review

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X Cheng. 1995. DNA modification by methyltransferases.. https://doi.org/10.1016/0959-440x(95)80003-j

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