Dual Roles of p300 in Chromatin Assembly and Transcriptional Activation in Cooperation with Nucleosome Assembly Protein 1 In Vitro

Asahara, Hiroshi; Tartare‐Deckert, Sophie; Nakagawa, Takeya; Ikehara, Tsuyoshi; Hirose, Fumiko; Hunter, Tony; Ito, Takashi; Montminy, Marc

doi:10.1128/mcb.22.9.2974-2983.2002

Cited by 81 publications

(93 citation statements)

References 53 publications

(77 reference statements)

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“…NAP1 enhances chromatin fluidity through exchanging histone dimers containing an H2A variant with H2A.Z variant and also interacts with transcriptional activators (25,38). Our results suggested that LPS stimulation in responsive cells promoted repositioning of nucleosomes 1 and 2 from the native/default position (R0) to an open/permissive position (R1).…”

Section: Pattern Of Nucleosome Positioning At the Human Tnf␣mentioning

confidence: 58%

Dynamic and Selective Nucleosome Repositioning during Endotoxin Tolerance

Gazzar

Liu

Yoza

et al. 2010

Journal of Biological Chemistry

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Sepsis is encoded by a sequel of transcription activation and repression events that initiate, sustain, and resolve severe systemic inflammation. The repression/silencing phase occurs in blood leukocytes of animals and humans following the initiation of systemic inflammation due to developing endotoxin tolerance. We previously reported that NF-B transcription factor RelB and histone H3 lysine methyltransferase G9a directly interact to induce facultative heterochromatin assembly and regulate epigenetic silencing during endotoxin tolerance, which is a major feature of sepsis. The general objective of this study was to assess whether dynamic temporal, structural, and positional changes of nucleosomes influence the sepsis phenotype. We used the THP-1 sepsis cell model to isolate mononucleosomes by rapid cell permeabilization and digestion of chromatin with micrococcal nuclease and then compared tumor necrosis factor ␣ (TNF␣) proximal promoter nucleosome alignment in endotoxin-responsive and -tolerant phenotypes. We found differential and dynamic repositioning of nucleosomes from permissive to repressive locations during the activation and silencing phases of transcription reprogramming and identified the following mechanisms that may participate in the process. 1) Two proximal nucleosomes repositioned to expose the primary NF-B DNA binding site in endotoxin-responsive cells, and this "promoter opening" required the ATP-independent chaperone NAP1 to replace the core histone H2A with the H2A.Z variant. 2) During RelB-dependent endotoxin tolerance, the two nucleosomes repositioned and masked the primary NF-B DNA binding site. 3) Small interfering RNA-mediated inhibition of RelB expression prevented repressive nucleosome repositioning and tolerance induction, but the "open" promoter required endotoxin-induced NF-B p65 promoter binding to initiate transcription, supporting the known requirement of p65 posttranslational modifications for transactivation. 4) Sustaining the permissive promoter state after RelB knockdown required ATP-dependent nucleosome remodeler BAF complex. Moreover, we found that forced expression of RelB in responsive cells induced repressive nucleosome positioning and silenced TNF␣ transcription, demonstrating the plasticity of nucleosome remodeling and its dependence on RelB. Our data suggest that nucleosome repositioning controls both the induction and epigenetic silencing phases of TNF␣ transcription associated with sepsis.

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Section: Pattern Of Nucleosome Positioning At the Human Tnf␣mentioning

confidence: 58%

Dynamic and Selective Nucleosome Repositioning during Endotoxin Tolerance

Gazzar

Liu

Yoza

et al. 2010

Journal of Biological Chemistry

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“…Therefore, the fate of NAP1 in the eviction reaction is unclear. NAP1 has previously been shown to physically interact with p300 and has been implicated in p300-mediated transcriptional activation (20,21). The histone acceptor in the supernatant is likely the DNA, which was added to all reactions as a nonspecific competitor (see Materials and Methods).…”

Section: Resultsmentioning

confidence: 99%

“…For simplicity, only one of the three vCREs is shown. We depict NAP physically associated with p300 based on published studies (20,21) and data not shown.…”

Section: Figmentioning

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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“…Thus, the ordered disassembly and reassembly of nucleosomes is an important paradigm in gene regulation. Chromatin remodeling depends on the recruitment of acetyltransferases that acetylate the four core histones, on the activity of chromatin‐remodeling complexes and on the capacity of histone chaperones to act as a histone acceptors, facilitating their removal from DNA to stimulate transcription (Ito et al , 2000; Asahara et al , 2002; Lorch et al , 2006; Adkins et al , 2007; Sharma & Nyborg, 2008). …”

Section: Introductionmentioning

confidence: 99%

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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Dual Roles of p300 in Chromatin Assembly and Transcriptional Activation in Cooperation with Nucleosome Assembly Protein 1 In Vitro

Cited by 81 publications

References 53 publications

Dynamic and Selective Nucleosome Repositioning during Endotoxin Tolerance

Dynamic and Selective Nucleosome Repositioning during Endotoxin Tolerance

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

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

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