The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding

Bonaldi, Tiziana; Längst, Gernot; Strohner, Ralf; Becker, Peter B.; Bianchi, Marco E.

doi:10.1093/emboj/cdf692

Cited by 239 publications

(179 citation statements)

References 65 publications

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“…H2A.Z-containing promoters have repositioned nucleosomes, whereas promoters lacking H2A.Z do not (57). Although this may not be the case with the TNF␣ promoter (because nucleosomes in native/default positions (R0 cells) were well positioned, yet they did not have H2A.Z), these previous studies and the current results clearly demonstrate that transcriptionally active chromatin is depleted in the H2A variant and that NAP1 plays an important role in histone exchange and nucleosomal sliding (24,60,61). Our finding that H2A.Z associated with H3K4me3 mark suggests that H2A.Z may influence the epigenetic nature of the target chromatin loci, as previously demonstrated (56).…”

Section: Discussioncontrasting

confidence: 40%

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: Discussioncontrasting

confidence: 40%

Dynamic and Selective Nucleosome Repositioning during Endotoxin Tolerance

Gazzar

Liu

Yoza

et al. 2010

Journal of Biological Chemistry

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“…Each box consists three α-helices that form an L shape. The A box or B box binds DNA in the minor groove despite of DNA sequence (Bonaldi et al, 2002). HMG boxes cause a significant bend in DNA and bind to the distorted DNA, such as four-way DNA junctions, cisplatin-damaged DNA and DNA mini-circles (Bianchi et al, 1989;Pil et al, 1992).…”

Section: Discussionmentioning

confidence: 99%

“…HMGB1 protein binds to minor groove of DNA and promotes the assembly of site-specific transcriptional proteins (Bonaldi et al, 2002). In addition to its well-established nuclear functions, HMGB1 protein functions as a extracellular signalling molecule which plays a criticle role in inflammation and carcinogenesis (Scaffidi et al, 2002;Ellerman et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

High Mobility Group Box 1 Protein Is Methylated and Transported to Cytoplasm in Clear Cell Renal Cell Carcinoma

Zhao²,

Ding³

et al. 2013

Asian Pacific Journal of Cancer Prevention

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Background:The high mobility group box 1 (HMGB1) protein is a widespread nuclear protein present in most cell types. It typically locates in the nucleus and functions as a nuclear cofactor in transcription regulation. However, HMGB1 can also localize in the cytoplasm and be released into extracellular matrix, where it plays critical roles in carcinogenesis and inflammation. However, it remains elusive whether HMGB1 is relocated to cytoplasm in clear cell renal cell carcinoma (ccRCC). Methods: Nuclear and cytoplasmic proteins were extracted by different protocols from 20 ccRCC samples and corresponding adjacent renal tissues. Western blotting and immunohistochemistry were used to identify the expression of HMGB1 in ccRCC. To elucidate the potential mechanism of HMGB1 cytoplasmic translocation, HMGB1 proteins were enriched by immunoprecipitation and analyzed by mass spectrometry (MS). Results: The HMGB1 protein was overexpressed and partially localized in cytoplasm in ccRCC samples (12/20, 60%, p<0.05). Immunohistochemistry results indicated that ccRCC of high nuclear grade possess more HMGB1 relocation than those with low grade (p<0.05). Methylation of HMGB1 at lysine 112 in ccRCC was detected by MS. Bioinformatics analysis showed that post-translational modification might affect the binding ability to DNA and mediate its translocation. Conclusion: Relocation of HMGB1 to cytoplasm was confirmed in ccRCC. Methylation of HMGB1 at lysine 112 might the redistribution of this cofactor protein.

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“…Non-histone architectural protein HMGB1 was found to regulate ACF remodeling activity by acting as a DNA chaperone that can facilitate rate limiting distortion of DNA. ACF translocates along DNA in the process of chromatin assembly [95]. Acf1 plays an important role in development as Acf1 null mutants were found to die during larval to pupal transition [96].…”

Section: Iswi Familymentioning

confidence: 99%

Mechanisms of ATP dependent chromatin remodeling

Gangaraju

Bartholomew

2007

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

128

159

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The inter-relationship between DNA repair and ATP dependent chromatin remodeling has begun to become very apparent with recent discoveries. ATP dependent remodeling complexes mobilize nucleosomes along DNA, promote the exchange of histones, or completely displace nucleosomes from DNA. These remodeling complexes are often categorized based on the domain organization of their catalytic subunit. The biochemical properties and structural information of several of these remodeling complexes are reviewed. The different models for how these complexes are able to mobilize nucleosomes and alter nucleosome structure are presented incorporating several recent findings. Finally the role of histone tails and their respective modifications in ATP-dependent remodeling are discussed.

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The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding

Cited by 239 publications

References 65 publications

Dynamic and Selective Nucleosome Repositioning during Endotoxin Tolerance

Dynamic and Selective Nucleosome Repositioning during Endotoxin Tolerance

High Mobility Group Box 1 Protein Is Methylated and Transported to Cytoplasm in Clear Cell Renal Cell Carcinoma

Mechanisms of ATP dependent chromatin remodeling

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