The DNA (Cytosine-5) Methyltransferases

Kumar, S., Cheng, X. D., Klimasauskas, S., Mi, S., Posfai, J., Roberts, R. J., Wilson, G. G. (January 1994) The DNA (Cytosine-5) Methyltransferases. Nucleic Acids Research, 22 (1). pp. 1-10. ISSN 0305-1048

URL: http://www.ncbi.nlm.nih.gov/pubmed/8127644
DOI: 10.1093/nar/22.1.1

Abstract

The m5C-MTases form a closely-knit family of enzymes in which common amino acid sequence motifs almost certainly translate into common structural and functional elements. These common elements are located predominantly in a single structural domain that performs the chemistry of the reaction. Sequence-specific DNA recognition is accomplished by a separate domain that contains recognition elements not seen in other structures. This, combined with the novel and unexpected mechanistic feature of trapping a base out of the DNA helix, makes the m5C-MTases an intriguing class of enzymes for further study. The reaction pathway has suddenly become more complicated because of the base-flipping and much remains to be learned about the DNA recognition elements in the family members for which structural information is not yet available.

Item Type: Paper
Uncontrolled Keywords: RESTRICTION-MODIFICATION SYSTEM TARGET-RECOGNIZING DOMAINS BACILLUS-SUBTILIS PHAGES AMINO-ACID-SEQUENCE NUCLEOTIDE-SEQUENCE MODIFICATION METHYLASE NEISSERIA-GONORRHOEAE MODIFICATION GENES ESCHERICHIA-COLI MOLECULAR CHARACTERIZATION
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase
CSHL Authors:
Communities: CSHL labs > Roberts lab
Depositing User: Matt Covey
Date: January 1994
Date Deposited: 08 May 2015 14:40
Last Modified: 08 May 2015 14:40
PMCID: PMC307737
Related URLs:
URI: http://repository.cshl.edu/id/eprint/31458

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