The DNA (cytosine-5) methyltransferases

• Published in: Nucleic acids research Vol. 22; no. 1; pp. 1 - 10
• Main Authors: Kumar, Sanjay, Cheng, Xiaodong, Klimasauskas, Saulius, Sha, Mi, Posfai, Janos, Roberts, Richard J., Wilson, Geoffrey G.
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 11.01.1994
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Biological and medical sciences; DNA-Cytosine Methylases - chemistry; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Models, Molecular; Molecular Sequence Data; Protein Structure, Tertiary; S-Adenosylmethionine - metabolism; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity; Transferases; Methyltransferases; Structural unit; Enzyme; Transferases; DNA (cytosine-5-)-methyltransferase; Molecular interaction; Review; Spatial structure; Aminoacid sequence; Structural analysis
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/22.1.1

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.