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-Structure paper
Title | Nucleosome recognition and DNA distortion by the Chd1 remodeler in a nucleotide-free state. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 29, Issue 2, Page 121-129, Year 2022 |
Publish date | Feb 16, 2022 |
Authors | Ilana M Nodelman / Sayan Das / Anneliese M Faustino / Stephen D Fried / Gregory D Bowman / Jean-Paul Armache / |
PubMed Abstract | Chromatin remodelers are ATP-dependent enzymes that reorganize nucleosomes within all eukaryotic genomes. Here we report a complex of the Chd1 remodeler bound to a nucleosome in a nucleotide-free ...Chromatin remodelers are ATP-dependent enzymes that reorganize nucleosomes within all eukaryotic genomes. Here we report a complex of the Chd1 remodeler bound to a nucleosome in a nucleotide-free state, determined by cryo-EM to 2.3 Å resolution. The remodeler stimulates the nucleosome to absorb an additional nucleotide on each strand at two different locations: on the tracking strand within the ATPase binding site and on the guide strand one helical turn from the ATPase motor. Remarkably, the additional nucleotide on the tracking strand is associated with a local transformation toward an A-form geometry, explaining how sequential ratcheting of each DNA strand occurs. The structure also reveals a histone-binding motif, ChEx, which can block opposing remodelers on the nucleosome and may allow Chd1 to participate in histone reorganization during transcription. |
External links | Nat Struct Mol Biol / PubMed:35173352 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.3 - 2.9 Å |
Structure data | EMDB-25479: 2.3 A structure of the ATP-dependent chromatin remodeler Chd1 bound to the nucleosome in a nucleotide-free state EMDB-25480: EMDB-25481: EMDB-25483: |
Source |
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Keywords | DNA BINDING PROTEIN/DNA / CHD1 / chromatin remodeling / ATPase / DBD / nucleosome / remodeling / transcription / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex |