The structure of nucleosome assembly protein 1

Park, Young-Jun; Luger, Karolin

doi:10.1073/pnas.0508002103

Cited by 193 publications

(294 citation statements)

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“…Our structure shows that histone binding through the yNap1 HBR regions and oligomerization through the IF1 and IF2 interfaces of the complex synergistically contribute to histone binding. Individual mutations in the HBR or NBR interfaces did not abolish H2A–H2B binding (Fig 3D and E) presumably due to the low nanomolar binding affinity between yNap1 and H2A–H2B (Park & Luger, 2006; Andrews et al , 2008). We observed reduced H2A–H2B binding only when both HBR regions contained charge reversal or alanine mutations (Fig 3D).…”

Section: Discussionmentioning

confidence: 96%

Structural evidence for Nap1‐dependent H2A–H2B deposition and nucleosome assembly

et al. 2016

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Nap1 is a histone chaperone involved in the nuclear import of H2A–H2B and nucleosome assembly. Here, we report the crystal structure of Nap1 bound to H2A–H2B together with in vitro and in vivo functional studies that elucidate the principles underlying Nap1‐mediated H2A–H2B chaperoning and nucleosome assembly. A Nap1 dimer provides an acidic binding surface and asymmetrically engages a single H2A–H2B heterodimer. Oligomerization of the Nap1–H2A–H2B complex results in burial of surfaces required for deposition of H2A–H2B into nucleosomes. Chromatin immunoprecipitation‐exonuclease (ChIP‐exo) analysis shows that Nap1 is required for H2A–H2B deposition across the genome. Mutants that interfere with Nap1 oligomerization exhibit severe nucleosome assembly defects showing that oligomerization is essential for the chaperone function. These findings establish the molecular basis for Nap1‐mediated H2A–H2B deposition and nucleosome assembly.

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Section: Discussionmentioning

confidence: 96%

Structural evidence for Nap1‐dependent H2A–H2B deposition and nucleosome assembly

et al. 2016

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“…1 and 2. The histone chaperone NAP1 has previously been shown to play a role in nucleosome assembly, exchange, and disassembly of the H2A/H2B dimer (17,18). Furthermore, NAP1 functions in an ATP-independent manner.…”

Section: Resultsmentioning

confidence: 99%

The coactivators CBP/p300 and the histone chaperone NAP1 promote transcription-independent nucleosome eviction at the HTLV-1 promoter

Sharma

Nyborg

2008

Proc. Natl. Acad. Sci. U.S.A.

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The human T cell leukemia virus type 1 (HTLV-1) is the causative agent of adult T cell leukemia/lymphoma. The multifunctional virally encoded oncoprotein Tax is responsible for malignant transformation and potent activation of HTLV-1 transcription. Tax, in complex with phosphorylated cAMP response element binding protein (pCREB), strongly recruits the cellular coactivators CREB binding protein (CBP)/p300 to the viral promoter concomitant with transcriptional activation. Although the mechanism of activator/coactivator-mediated transcriptional activation is poorly understood, the recruitment of CBP/p300 by regulatory factors appears to function, in part, by promoting changes in chromatin architecture that are permissive to transcriptional activation. Here, we show that CBP/p300 recruitment promotes histone acetylation and eviction of the histone octamer from the chromatin-assembled HTLV-1 promoter template in vitro. Nucleosome disassembly is strictly acetyl-CoA dependent and is not linked to ATP utilization. We find that the histone chaperone, nucleosome assembly protein 1 (NAP1), cooperates with CBP/p300 in eviction of the acetylated histones from the chromatin template. These findings reveal a unique mechanism in which the DNA-bound Tax/pCREB complex recruits CBP/p300, and together with NAP1, the coactivators cooperate to dramatically reduce nucleosome occupancy at the viral promoter in an acetylation-dependent and transcription-independent fashion.Tax ͉ cAMP response element binding protein ͉ acetylation ͉ chromatin ͉ histone acetyltransferase

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“…NUCLEOSOME ASSEMBLY PROTEIN1 (NAP1) belongs to a family of evolutionarily conserved histone chaperones. NAP1 binds all types of histones in vitro and is found primarily associated with H2A/H2B in vivo and thus is considered as an H2A/ H2B-type histone chaperone (Dong et al, 2003(Dong et al, , 2005Park and Luger, 2006;Zhu et al, 2006). NAP1 proteins are implicated in histone trafficking (Mosammaparast et al, 2002;Miyaji-Yamaguchi et al, 2003;Dong et al, 2005), nucleosome assembly (Ito et al, 1996;Andrews et al, 2010), and disassembly (Lorch et al, 2006;Walfridsson et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

NAP1 Family Histone Chaperones Are Required for Somatic Homologous Recombination in Arabidopsis

et al. 2012

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Homologous recombination (HR) is essential for maintaining genome integrity and variability. To orchestrate HR in the context of chromatin is a challenge, both in terms of DNA accessibility and restoration of chromatin organization after DNA repair. Histone chaperones function in nucleosome assembly/disassembly and could play a role in HR. Here, we show that the NUCLEOSOME ASSEMBLY PROTEIN1 (NAP1) family histone chaperones are required for somatic HR in Arabidopsis thaliana. Depletion of either the NAP1 group or NAP1-RELATED PROTEIN (NRP) group proteins caused a reduction in HR in plants under normal growth conditions as well as under a wide range of genotoxic or abiotic stresses. This contrasts with the hyperrecombinogenic phenotype caused by the depletion of the CHROMATIN ASSEMBLY FACTOR-1 (CAF-1) histone chaperone. Furthermore, we show that the hyperrecombinogenic phenotype caused by CAF-1 depletion relies on NRP1 and NRP2, but the telomere shortening phenotype does not. Our analysis of DNA lesions, H3K56 acetylation, and expression of DNA repair genes argues for a role of NAP1 family histone chaperones in nucleosome disassembly/reassembly during HR. Our study highlights distinct functions for different families of histone chaperones in the maintenance of genome stability and establishes a crucial function for NAP1 family histone chaperones in somatic HR.

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The structure of nucleosome assembly protein 1

Cited by 193 publications

References 50 publications

Structural evidence for Nap1‐dependent H2A–H2B deposition and nucleosome assembly

Structural evidence for Nap1‐dependent H2A–H2B deposition and nucleosome assembly

The coactivators CBP/p300 and the histone chaperone NAP1 promote transcription-independent nucleosome eviction at the HTLV-1 promoter

NAP1 Family Histone Chaperones Are Required for Somatic Homologous Recombination in Arabidopsis

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