Histone chaperones in nucleosome eviction and histone exchange

Park, Young-Jun; Luger, Karolin

doi:10.1016/j.sbi.2008.04.003

Cited by 172 publications

(152 citation statements)

References 63 publications

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“…Moreover, NP interacts with and displaces chromatinbound linker histones H1, H5 (erythrocytes specific linker histones), and B4 (Xenopus embryonic linker histones) (8,9). This behavior has also been observed for other histone chaperones belonging to different protein families (NAP-1 and TAF-I) (3,6,10,11).…”

Section: Nucleoplasmin (Npmentioning

confidence: 60%

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Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face*

Ramos

Martín‐Benito

Finn

et al. 2010

Journal of Biological Chemistry

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Nucleoplasmin (NP) is a pentameric chaperone that regulates the condensation state of chromatin extracting specific basic proteins from sperm chromatin and depositing H2A-H2B histone dimers. It has been proposed that histones could bind to either the lateral or distal face of the pentameric structure. Here, we combine different biochemical and biophysical techniques to show that natural, hyperphosphorylated NP can bind five H2A-H2B dimers and that the amount of bound ligand depends on the overall charge (phosphorylation level) of the chaperone. Three-dimensional reconstruction of NP/H2A-H2B complex carried out by electron microscopy reveals that histones interact with the chaperone distal face. Limited proteolysis and mass spectrometry indicate that the interaction results in protection of the histone fold and most of the H2A and H2B C-terminal tails. This structural information can help to understand the function of NP as a histone chaperone.

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Section: Nucleoplasmin (Npmentioning

confidence: 60%

“…Histone chaperones shield the positive charge of bound histones, allowing their proper deposition onto DNA in the chromatin assembly process (3,6). NP regulates the condensation state of chromatin by extracting sperm-specific basic proteins from DNA and depositing H2A-H2B dimers.…”

Section: Nucleoplasmin (Npmentioning

confidence: 99%

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face*

Ramos

Martín‐Benito

Finn

et al. 2010

Journal of Biological Chemistry

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“…Nucleosome replacement requires that old histones dissociate from DNA and that new histones repackage the exposed DNA. In vivo, this process requires factors that manipulate DNA-histone contacts to unwrap the nucleosome, and protein chaperones to remove and deliver histones (32). Chromatin remodelers can contribute to nucleosome assembly by unwrapping and rebuilding nucleosomes (33).…”

Section: Discussionmentioning

confidence: 99%

The XNP remodeler targets dynamic chromatin in Drosophila

Schneiderman

Sakai

Goldstein

et al. 2009

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

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Heterochromatic gene silencing results from the establishment of a repressive chromatin structure over reporter genes. Gene silencing is often variegated, implying that chromatin may stochastically switch from repressive to permissive structures as cells divide. To identify remodeling enzymes involved in reorganizing heterochromatin, we tested 11 SNF2-type chromatin remodelers in Drosophila for effects on gene silencing. Overexpression of five remodelers affects gene silencing, and the most potent de-repressor is the ␣-thalassaemia mental retardation syndrome X-linked (ATRX) homolog X-linked nuclear protein (XNP). Although the mammalian ATRX protein localizes to heterochromatin, Drosophila XNP is not a general component of heterochromatin. Instead, XNP localizes to active genes and to a major focus near the heterochromatin of the X chromosome. The XNP focus corresponds to an unusual decondensed satellite DNA block, and both active genes and the XNP focus are sites of ongoing nucleosome replacement. We suggest that the XNP remodeler modulates nucleosome dynamics at its target sites to limit chromatin accessibility. Although XNP at active genes may contribute to gene silencing, we find that a single focus is present across Drosophila species and that perturbation of this site cripples heterochromatic gene silencing. Thus, the XNP focus appears to be a functional genetic element that can contribute to gene silencing throughout the nucleus.heterochromatin ͉ nucleosome dynamics ͉ chromatin remodelers C hromatin in the eukaryotic nucleus consists of DNA wrapped around histone octamers into nucleosomes. Cytological and molecular features distinguish different kinds of chromatin within the nucleus (1). Gene-rich regions are usually packaged into euchromatin, which is decondensed in interphase nuclei, enriched for histone modifications associated with transcriptional activity, and often has high DNA accessibility. In contrast, gene-poor and repetitive sequences are packaged into heterochromatin, a condensed, relatively inaccessible chromatin organization that carries histone modifications associated with transcriptional repression.The genetic phenomenon of position effect variegation first indicated that heterochromatin could affect gene activity (2). Heterochromatic gene silencing has served as a sensitive measure to identify mutations in components of chromatin-based regulation (3, 4). Transcriptional repression in heterochromatin is thought to be crucial to limit the accumulation of transposable elements and unstable repetitive sequences in genomes.A major class of factors involved in altering chromatin structure is the SNF2-type chromatin remodelers (named after the founding sucrose nonfermenting 2 protein in Saccharomyces cerevisiae) (5). These nuclear enzymes use the energy of ATP binding and hydrolysis to manipulate histone-DNA contacts in nucleosomes. Individual remodelers also appear to differ in their activities; whereas some have been implicated in regulating promoter accessibility (6, 7), others are required ...

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“…Histones are highly conserved across all eukaryotic cells,2 and act as nuclear chaperone proteins, interacting with nucleic acids due to their highly positive charge3 from lysine and arginine residues. Each nucleosome particle consists of 147 base pairs of DNA, wrapped in 1.7 turns around a protein octamer of core histones (H2A, H2B, H3 and H4), further compacted by linker histones (H1 and/or H5) 4…”

Section: Introductionmentioning

confidence: 99%

Biology, role and therapeutic potential of circulating histones in acute inflammatory disorders

Szatmary

Huang

Criddle

et al. 2018

J Cellular Molecular Medi

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Histones are positively charged nuclear proteins that facilitate packaging of DNA into nucleosomes common to all eukaryotic cells. Upon cell injury or cell signalling processes, histones are released passively through cell necrosis or actively from immune cells as part of extracellular traps. Extracellular histones function as microbicidal proteins and are pro‐thrombotic, limiting spread of infection or isolating areas of injury to allow for immune cell infiltration, clearance of infection and initiation of tissue regeneration and repair. Histone toxicity, however, is not specific to microbes and contributes to tissue and end‐organ injury, which in cases of systemic inflammation may lead to organ failure and death. This review details the processes of histones release in acute inflammation, the mechanisms of histone‐related tissue toxicity and current and future strategies for therapy targeting histones in acute inflammatory diseases.

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Histone chaperones in nucleosome eviction and histone exchange

Cited by 172 publications

References 63 publications

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face*

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face*

The XNP remodeler targets dynamic chromatin in Drosophila

Biology, role and therapeutic potential of circulating histones in acute inflammatory disorders

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