The activity of the murine DNA methyltransferase Dnmt1 is controlled by interaction of the catalytic domain with the N-terminal part of the enzyme leading to an allosteric activation of the enzyme after binding to methylated DNA

Journal of Molecular Biology

Volumn 309, Issue 5, 2001, Pages 1189-1199

  Fatemi, Mehrnaz ^a   Hermann, Andrea ^a   Pradhan, Shriharsa ^b   Jeltsch, Albert ^a  

^a JUSTUS LIEBIG UNIVERSITY   (Germany)

^b NEW ENGLAND BIOLABS   (United States)

Author keywords

DNA methylation; Enzyme specificity; Epigenetics; Gene regulation; Maintenance methylation

Indexed keywords

AMINO ACID; BINDING PROTEIN; DNA METHYLTRANSFERASE;

AGING; ALLOSTERISM; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BACULOVIRUS; CARCINOGENESIS; CATALYSIS; DNA BINDING; DNA METHYLATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION;

INSECTA; MAMMALIA; MURINAE; UNIDENTIFIED BACULOVIRUS;

EID: 0035933336     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4709     Document Type: Article

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