Histone chaperones: 30 years from isolation to elucidation of the mechanisms of nucleosome assembly and disassembly

Eitoku, Masamitsu; Sato, Lui; Senda, Toshiya; Horikoshi, Masami

doi:10.1007/s00018-007-7305-6

Cited by 181 publications

(208 citation statements)

References 327 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%

“…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%

“…5 or NPM2) belongs to the so called "histone chaperone" or "nuclear chaperone" group of proteins that, together with other chromatin remodeling complexes, are responsible for chromatin remodeling events during cell division, apoptosis, fertilization, DNA damage repair, etc. (1)(2)(3)(4)(5).…”

mentioning

confidence: 99%

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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%

Section: Nucleoplasmin (Npmentioning

confidence: 99%

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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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“…The elegant genetic studies cited above have largely been focused on cooperative and/or overlapping roles for N-tails of either H2A/H2B or H3/H4 pairs, likely because of their well-known, pairwise association during nucleosome assembly/disassembly and structural features of assembled nucleosomal octamers (1,20). Interestingly, however, sequence similarity exists on the N-tails of H2A and H4, notably the extreme amino-terminal residues are nearly identical between the two (underlined in Fig.…”

mentioning

confidence: 99%

Mutagenesis of pairwise combinations of histone amino-terminal tails reveals functional redundancy in budding yeast

Kim

Hsu

Smith

et al. 2012

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

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A large body of literature provides compelling evidence for the role of evolutionarily conserved core histone residues in various biological processes. However, site-directed mutagenesis of individual residues that are known to be sites of posttranslational modifications often does not result in clear phenotypic defects. In some cases, the combination of multiple mutations can give rise to stronger phenotypes, implying functional redundancy between distinct residues on histones. Here, we examined the “histone redundancy hypothesis” by characterizing double deletion of all pairwise combinations of amino-terminal tails (N-tails) from the four core histones encoded in budding yeast. First, we found that multiple lysine residues on the N-tails of both H2A and H4 are redundantly involved in cell viability. Second, simultaneous deletion of N-tails from H2A and H3 leads to a severe growth defect, which is correlated with perturbed gross chromatin structure in the mutant cells. Finally, by combining point mutations on H3 with deletion of the H2A N-tail, we revealed a redundant role for lysine 4 on H3 and the H2A N-tail in hydroxyurea-mediated response. Altogether, these data suggest that the N-tails of core histones share previously unrecognized, potentially redundant functions that, in some cases are different from those of the widely accepted H2A/H2B and H3/H4 dimer pairs.

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“…Chromatin assembly is a stepwise process that requires histone chaperones to deposit histones in forming nucleosomes. These chaperones are essential to facilitate ordered assembly of nucleosomes for both replication-dependent and -independent events (1).…”

mentioning

confidence: 99%

Transcription factor EKLF (KLF1) recruitment of the histone chaperone HIRA is essential for β-globin gene expression

Soni

Pchelintsev

Adams

et al. 2014

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

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The binding of chromatin-associated proteins and incorporation of histone variants correlates with alterations in gene expression. These changes have been particularly well analyzed at the mammalian β-globin locus, where transcription factors such as erythroid Krüppel-like factor (EKLF), which is also known as Krüppel-like factor 1 (KLF1), play a coordinating role in establishing the proper chromatin structure and inducing high-level expression of adult β-globin. We had previously shown that EKLF preferentially interacts with histone H3 and that the H3.3 variant is differentially recruited to the β-globin promoter. We now find that a novel interaction between EKLF and the histone cell cycle regulation defective homolog A (HIRA) histone chaperone accounts for these effects. HIRA is not only critical for β-globin expression but is also required for activation of the erythropoietic regulators EKLF and GATA binding protein 1 (GATA1). Our results provide a mechanism by which transcription factor-directed recruitment of a generally expressed histone chaperone can lead to tissue-restricted changes in chromatin components, structure, and transcription at specific genomic sites during differentiation.

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Histone chaperones: 30 years from isolation to elucidation of the mechanisms of nucleosome assembly and disassembly

Cited by 181 publications

References 327 publications

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

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

Mutagenesis of pairwise combinations of histone amino-terminal tails reveals functional redundancy in budding yeast

Transcription factor EKLF (KLF1) recruitment of the histone chaperone HIRA is essential for β-globin gene expression

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