Dissection of structure and function of the N-terminal domain of mouse DNMT1 using regional frame-shift mutagenesis

• Published in: PloS one Vol. 5; no. 3; p. e9831
• Main Authors: D'Aiuto, Leonardo, Marzulli, Marco, Mohan, K Naga, Borowczyk, Ewa, Saporiti, Federica, Vandemark, Andrew, Chaillet, J Richard
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 23.03.2010; Public Library of Science (PLoS)
• Subjects: Amino acid sequence; Amino acids; Animals; Binding sites; Deletion mutant; Developmental Biology/Stem Cells; Directed evolution; Dissection; DNA (Cytosine-5-)-Methyltransferase 1; DNA (Cytosine-5-)-Methyltransferases - metabolism; DNA methylation; DNA, Complementary - metabolism; DNMT1 protein; Embryonic Stem Cells - cytology; Enzymatic activity; Evolutionary design method; Frameshift Mutation; Gene Deletion; Genetics and Genomics/Epigenetics; Genetics and Genomics/Gene Expression; Genetics and Genomics/Gene Function; Immunohistochemistry - methods; Methylation; Methyltransferase; Methyltransferases; Mice; Molecular Biology/Chromatin Structure; Molecular Biology/DNA Methylation; Mutagenesis; Mutagenesis, Site-Directed; Mutants; Mutation; Plasmids - metabolism; Protein Folding; Protein structure; Protein Structure, Tertiary; Regional analysis; Regional development; Stem cells; Structural stability; Structure-function relationships; Surgery; Transcription, Genetic; Pittsburgh Pennsylvania; Pennsylvania

Deletion analysis of mouse DNMT1, the primary maintenance methyltransferase in mammals, showed that most of the N-terminal regulatory domain (amino acid residues 412-1112) is required for its enzymatic activity. Although analysis of deletion mutants helps to identify regions of a protein sequence re...