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Mol Cell
2017 Feb 02;653:447-459.e6. doi: 10.1016/j.molcel.2016.12.011.
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Interdomain Communication of the Chd1 Chromatin Remodeler across the DNA Gyres of the Nucleosome.
Nodelman IM
,
Bleichert F
,
Patel A
,
Ren R
,
Horvath KC
,
Berger JM
,
Bowman GD
.
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Chromatin remodelers use a helicase-like ATPase motor to reposition and reorganize nucleosomes along genomic DNA. Yet, how the ATPase motor communicates with other remodeler domains in the context of the nucleosome has so far been elusive. Here, we report for the Chd1 remodeler a unique organization of domains on the nucleosome that reveals direct domain-domain communication. Site-specific cross-linking shows that the chromodomains and ATPase motor bind to adjacent SHL1 and SHL2 sites, respectively, on nucleosomal DNA and pack against the DNA-binding domain on DNA exiting the nucleosome. This domain arrangement spans the two DNA gyres of the nucleosome and bridges both ends of a wrapped, ∼90-bp nucleosomal loop of DNA, suggesting a means for nucleosome assembly. This architecture illustrates how Chd1 senses DNA outside the nucleosome core and provides a basis for nucleosome spacing and directional sliding away from transcription factor barriers.
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