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Literature DB >> 27273866

Coordinated Action of Nap1 and RSC in Disassembly of Tandem Nucleosomes.

Rashmi Prasad¹, Sheena D'Arcy², Arjan Hada³, Karolin Luger⁴, Blaine Bartholomew⁵.

Abstract

The SWI/SNF and RSC family of ATP-dependent chromatin remodelers disassembles nucleosomes by moving nucleosomes into the vicinity of adjoining nucleosomes. We found that the histone chaperone Nap1 efficiently promotes disassembly of adjacent nucleosomes with which RSC collides and not the disassembly of nucleosomes mobilized by RSC. Nap1 is specific to RSC, as it does not target SWI/SNF, its paralog in Saccharomyces cerevisiae Extensive mutational analysis of Nap1 has revealed that Nap1 affinity for histones H2A-H2B and H3-H4 and its ability to displace histones from DNA are required for Nap1 to enhance RSC-mediated disassembly. Other histone chaperones, such as Vps75, that also bind histones are not able to enhance RSC-mediated disassembly. Our study suggests a mechanism by which Nap1 is recruited to actively transcribed regions and assists in the passage of the transcription complex through chromatin, and it provides a novel mechanism for the coordinated action of RSC and Nap1.

Entities: Chemical Gene Species

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Year: 2016 PMID： 27273866 PMCID： PMC4985928 DOI： 10.1128/MCB.00195-16

Source DB: PubMed Journal: Mol Cell Biol ISSN： 0270-7306 Impact factor: 4.272

47 in total

Coordinated Action of Nap1 and RSC in Disassembly of Tandem Nucleosomes.

1. Genome-wide location and regulated recruitment of the RSC nucleosome-remodeling complex.

2. SWI/SNF unwraps, slides, and rewraps the nucleosome.

3. Control of neurulation by the nucleosome assembly protein-1-like 2.

4. Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes.

Review 5. The histone shuffle: histone chaperones in an energetic dance.

6. Knockout targeting of the Drosophila nap1 gene and examination of DNA repair tracts in the recombination products.

7. The histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone DNA interactions.

8. A protein which facilitates assembly of nucleosome-like structures in vitro in mammalian cells.

9. Architecture of the SWI/SNF-nucleosome complex.

10. The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation.

1. Nucleosome composition regulates the histone H3 tail conformational ensemble and accessibility.

2. DNA sequence influences hexasome orientation to regulate DNA accessibility.

3. Inhibition of transcription leads to rewiring of locus-specific chromatin proteomes.