The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains

Ryan, Daniel P.; Sundaramoorthy, Ramasubramanian; Martin, David; Singh, Vijender; Owen-Hughes, Tom

doi:10.1038/emboj.2011.166

Cited by 110 publications

(143 citation statements)

References 63 publications

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“…ISWI-type remodelers have significant sequence homology to the C-terminal bridge segment following the Chd1 ATPase motor, suggesting that they too possess a similar structure (17). Likewise, the DNA-binding domain of Chd1 was found to consist of a SANT and SLIDE domain pair, analogous to the HAND-SANT-SLIDE DNA-binding domain first reported for ISWI (24,38). Given the importance of the ATPase coupling residues described here for nucleosome sliding, one might expect ISWI remodelers to possess a functionally similar element.…”

Section: Discussionmentioning

confidence: 96%

“…Using a fluorescently labeled peptide encompassing residues 932-955, we were unable to detect interactions with mononucleosomes using native PAGE (data not shown). If this region were to contact the nucleosome, similar to the scenarios proposed for the Chd1 DNA-binding domain (24), these residues might be important for the remodeler to maintain a grip on the nucleosomal substrate during the sliding reaction. Alternatively, and analogously to PcrA, these residues might be important for destabilizing histone-DNA or histone-histone interactions required for nucleosome sliding.…”

Section: Discussionmentioning

confidence: 99%

“…In yeast Chd1, structural information is now available for the chromodomain-ATPase motor (17) and the DNA-binding domain (24). Approximately 87 amino acid residues separate the ATPase motor (which includes a ϳ50 residue C-terminal bridge segment that folds against the ATPase core and ends around residue 922) from the DNA-binding domain (residues 1009 -1274).…”

Section: A Segment Between Atpase Motor and Dna-binding Domains Of Chd1mentioning

confidence: 99%

“…The DNA-binding domain is needed for the Chd1 remodeler to stably associate with nucleosomes, and this interaction requires extranucleosomal DNA (24). To see whether the deletion ⌬932-940 influenced the ability of Chd1 to associate with nucleosomes containing extranucleosomal DNA, increasing concentrations of both Chd1 ⌬NC and Chd1 ⌬NC ⌬932-940 were incubated with (0-N-63) nucleosomes and monitored by native PAGE (Fig.…”

Section: Deletion Of Residues 932-940 Does Notmentioning

confidence: 99%

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Identification of Residues in Chromodomain Helicase DNA-Binding Protein 1 (Chd1) Required for Coupling ATP Hydrolysis to Nucleosome Sliding

Patel

McKnight

Genzor

et al. 2011

Journal of Biological Chemistry

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Background: Chromatin remodelers slide nucleosomes in an ATP-dependent manner. Results: Residues between the ATPase motor and DNA-binding domain of chromodomain helicase DNA-binding protein 1 (Chd1) are required for sliding but not nucleosome-stimulated ATP hydrolysis. Conclusion: Residues outside the conserved ATPase core are required for efficiently utilizing the energy of ATP hydrolysis for sliding. Significance: Understanding the role of ATPase-coupling residues will be critical for revealing nucleosome sliding mechanisms.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Section: A Segment Between Atpase Motor and Dna-binding Domains Of Chd1mentioning

confidence: 99%

Section: Deletion Of Residues 932-940 Does Notmentioning

confidence: 99%

See 2 more Smart Citations

Identification of Residues in Chromodomain Helicase DNA-Binding Protein 1 (Chd1) Required for Coupling ATP Hydrolysis to Nucleosome Sliding

Patel

McKnight

Genzor

et al. 2011

Journal of Biological Chemistry

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“…1). CHD1 and CHD2 contain DNA-binding domains, which have been shown to be similar in function to SWI3, ADA2, N-COR, and TFIIB (SANT) domains present in CHD6-9 [18]. The SANT domain confers nonspecific DNA binding, particularly to linker DNA between nucleosomes [19][20][21].…”

Section: Structure and Function Of The Chd Superfamilymentioning

confidence: 99%

Chromodomain Helicase DNA-Binding Proteins in Stem Cells and Human Developmental Diseases

Micucci

Sperry

Martin

2015

Stem Cells and Development

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Rise of the Chromodomain Helicase DNA‐Binding (CHD) Chromatin Remodelling Machines

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2023

Encyclopedia of Life Sciences

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Vital processes such as transcription, repair, replication and recombination continuously shape cellular chromatin landscape. The chromodomain helicase DNA‐binding (CHD) family of enzymes regulate chromatin dynamics by utilising energy from ATP hydrolysis to alter nucleosomal position, structure and composition, thereby modulating accessibility of the underlying DNA sequence. The CHD enzymes are highly conserved in evolution, and genetic studies in fungi, plants and animals demonstrate their critical roles in regulation of cellular identity and fate and organismal development. Advances in genomic studies over the past two decades led to the identification of frequent DNA copy‐number alterations, mutations and aberrant expression of CHDs in human malignancies and various disorders, highlighting their importance as relevant biomarkers or targets for therapeutic intervention. Key Concepts CHD family of enzymes (CHD1‐9) are evolutionary conserved ATP‐dependent chromatin remodelers that mobilise nucleosomes to regulate DNA‐templated processes, such as transcription, replication and repair. They are critical for normal organismal development and are frequently mutated in human disorders and cancers. Chromodomain helicase DNA‐binding proteins (CHD1‐9) are evolutionary conserved family of ATP‐dependent chromatin remodelers that mobilise nucleosomes to regulate DNA‐templated processes such as transcription, replication and DNA repair. CHD enzymes share a common domain structure: two N‐terminal chromodomains, a central ATPase/helicase domain, and a C‐terminal DNA‐binding domain. CHD proteins play crucial roles in diverse cellular processes, including embryonic development, stem cell maintenance and differentiation, and tissue‐specific gene expression. Dysregulation of CHD proteins has been associated with various human diseases, including cancer and neurodevelopmental disorders. CHD proteins are attractive targets for the development of new therapies for diseases associated with chromatin dysfunction. Understanding the molecular mechanisms underlying the function of CHD proteins may pave the way for the development of new drugs that target these proteins and improve the treatment of a variety of human diseases.

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The DNA-binding domain of the Chd1 chromatin-remodelling enzyme contains SANT and SLIDE domains

Cited by 110 publications

References 63 publications

Identification of Residues in Chromodomain Helicase DNA-Binding Protein 1 (Chd1) Required for Coupling ATP Hydrolysis to Nucleosome Sliding

Identification of Residues in Chromodomain Helicase DNA-Binding Protein 1 (Chd1) Required for Coupling ATP Hydrolysis to Nucleosome Sliding

Chromodomain Helicase DNA-Binding Proteins in Stem Cells and Human Developmental Diseases

Rise of the Chromodomain Helicase DNA‐Binding (CHD) Chromatin Remodelling Machines

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