The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains
Copyright policy )The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains
The ATP-dependent chromatin-remodelling enzyme Chd1 is a 168-kDa protein consisting of a double chromodomain, Snf2-related ATPase domain, and a C-terminal DNA-binding domain. Here, we show the DNA-binding domain is required for Saccharomyces cerevisiae Chd1 to bind and remodel nucleosomes. The crystal structure of this domain reveals the presence of structural homology to SANT and SLIDE domains previously identified in ISWI remodelling enzymes. The presence of these domains in ISWI and Chd1 chromatin-remodelling enzymes may provide a means of efficiently harnessing the action of the Snf2-related ATPase domain for the purpose of nucleosome spacing and provide an explanation for partial redundancy between these proteins. Site directed mutagenesis was used to identify residues important for DNA binding and generate a model describing the interaction of this domain with DNA. Through inclusion of Chd1 sequences in homology searches SLIDE domains were identified in CHD6-9 proteins. Point mutations to conserved amino acids within the human CHD7 SLIDE domain have been identified in patients with CHARGE syndrome.
- Australian National University Australia
- University of Dundee United Kingdom
Models, Molecular, NUCLEOSOME, Crystallography, X-Ray, protein chd1, SACCHAROMYCES-CEREVISIAE, TRANSCRIPTION, IN-VIVO, Phylogeny, article, protein domain, CHROMODOMAINS, unclassified drug, Nucleosomes, DNA-Binding Proteins, priority journal, COMPLEXES, point mutation, PROTEIN-STRUCTURE, Protein Binding, crystal structure, 570, Saccharomyces cerevisiae Proteins, Molecular Sequence Data, Saccharomyces cerevisiae, protein DNA binding, SLIDE, Models, Biological, Article, site directed Chd1, Humans, Point Mutation, YEAST, Protein Interaction Domains and Motifs, human, Amino Acid Sequence, protein structure, DNA binding, Protein Structure, Quaternary, ACF, Keywords: protein, nonhuman, Binding Sites, Organisms, Genetically Modified, SANT, nucleotide sequence, Chd1, Chromatin Assembly and Disassembly, Protein Structure, Tertiary, ISWI, protein analysis, nucleosomes, CHARGE Syndrome
Models, Molecular, NUCLEOSOME, Crystallography, X-Ray, protein chd1, SACCHAROMYCES-CEREVISIAE, TRANSCRIPTION, IN-VIVO, Phylogeny, article, protein domain, CHROMODOMAINS, unclassified drug, Nucleosomes, DNA-Binding Proteins, priority journal, COMPLEXES, point mutation, PROTEIN-STRUCTURE, Protein Binding, crystal structure, 570, Saccharomyces cerevisiae Proteins, Molecular Sequence Data, Saccharomyces cerevisiae, protein DNA binding, SLIDE, Models, Biological, Article, site directed Chd1, Humans, Point Mutation, YEAST, Protein Interaction Domains and Motifs, human, Amino Acid Sequence, protein structure, DNA binding, Protein Structure, Quaternary, ACF, Keywords: protein, nonhuman, Binding Sites, Organisms, Genetically Modified, SANT, nucleotide sequence, Chd1, Chromatin Assembly and Disassembly, Protein Structure, Tertiary, ISWI, protein analysis, nucleosomes, CHARGE Syndrome
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