Modulation of chromatin function through linker histone H1 variants

Kowalski, Andrzej; Pałyga, Jan

doi:10.1111/boc.201600007

Cited by 20 publications

(21 citation statements)

References 154 publications

(260 reference statements)

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“…H1 variants are modified and regulated by PTMs 26 (BOX 1), but these modifications and their functional differences and importance are understudied compared with PTMs of core histone. Nevertheless, some interesting functional data are now starting to emerge.…”

Section: Linker Histone Variantsmentioning

confidence: 99%

Emerging roles of linker histones in regulating chromatin structure and function

Fyodorov

Zhou

Skoultchi

et al. 2017

Nat Rev Mol Cell Biol

295

328

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Together with core histones, which make up the nucleosome, the linker histone (H1) is one of the five main histone protein families present in chromatin in eukaryotic cells. H1 binds to the nucleosome to form the next structural unit of metazoan chromatin, the chromatosome, which may help chromatin to fold into higher-order structures. Despite their important roles in regulating the structure and function of chromatin, linker histones have not been studied as extensively as core histones. Nevertheless, substantial progress has been made recently. The first near-atomic resolution crystal structure of a chromatosome core particle and an 11 Å resolution cryo-electron microscopy-derived structure of the 30 nm nucleosome array have been determined, revealing unprecedented details about how linker histones interact with the nucleosome and organize higher-order chromatin structures. Moreover, several new functions of linker histones have been discovered, including their roles in epigenetic regulation and the regulation of DNA replication, DNA repair and genome stability. Studies of the molecular mechanisms of H1 action in these processes suggest a new paradigm for linker histone function beyond its architectural roles in chromatin.

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Section: Linker Histone Variantsmentioning

confidence: 99%

Emerging roles of linker histones in regulating chromatin structure and function

Fyodorov

Zhou

Skoultchi

et al. 2017

Nat Rev Mol Cell Biol

295

328

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“…As was shown by Kowalski and Pałyga (2014), the phenotype b2 belonging to the subtype H1.b did not occur in the duck production line, contrary to the histone H1.z phenotype z2, which is present in the duck conservative groups only. Thus, the peculiar histone H1 isoform constituting a given phenotype may evoke a special effect in the chromatin milieu promoting its unique local conformation and function (Kowalski and Pałyga, 2016), which affects breeding conditions and physiological features of the organism.…”

Section: Discussionmentioning

confidence: 99%

“…A specific activity of histone H1 subtypes, possessing characteristic genomic distribution (Izzo et al, 2013) and distinct rate of the mobility (Th'ng et al, 2005), is related to the differences in the ability to bind DNA and condense chromatin. The data originating from distinct reports (for a review, see Kowalski and Pałyga, 2016) indicate that the strong (histone H1.4 and H1.5), intermediary (histone H1.3) and weak (histone H1.1 and H1.2) chromatin condensers can be distinguished within the mammalian histone H1 subtypes. However, both common and individual impact on gene expression is characteristic for H1 histones.…”

Section: Introductionmentioning

confidence: 99%

“…There are also H1 subtype expressions which are confined to the specialized tissue and to the stage of cell differentiation (Parseghian, 2015;Kowalski and Pałyga, 2016). Mammalian histone H1 non-allelic subtypes are ubiquitously expressed in the somatic cells (H1.1, H1.2, H1.3, H1.4, H1.5, H1.0 and H1.10) and also characteristic for germ cells, present in the sperm (H1t, H1T2 and HILS1) and in the oocyte (H1oo) (Happel and Doenecke, 2009).…”

Section: Introductionmentioning

confidence: 99%

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Evidence on the stability of histone H1.a polymorphic variants during selection in quail

Kowalski

Knaga²

2017

Arch. Anim. Breed.

Self Cite

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Abstract. The goal of this work was to check whether selection for quantitative traits may cause a change in the histone H1 allelic complement and whether it can therefore be considered a modulator of histone H1-dependent chromatin functioning. For this purpose, a fluctuation of histone H1.a polymorphic variants was analyzed among a non-selected (control) quail line and the line selected for a high cholesterol content in the egg yolk. The histone H1.a was found to be polymorphic due to its differential migration rate in the AU-PAGE (acetic acidurea polyacrylamide gel electrophoresis). Based on this, two H1.a isoforms (H1.a1 and H1.a2) that form three phenotypes (a1, a2 and a1a2) were distinguished in the quail lines tested. A comparably expressed (p > 0.05) and low relative variable (coefficient of variation, CV < 0.25) histone H1.a phenotypes were in agreement with Hardy-Weinberg equilibrium (HWE) in both the non-selected (χ 2 = 1.29, p = 0.25) and selected (χ 2 = 1.9, p = 0.16) quail line. The similarity among quail lines was assessed based on the equal distribution of histone H1.a phenotypes (χ 2 = 1.63, p = 0.44) and alleles (χ 2 = 0.018, p = 0.89) frequency in both quail lines tested. This indicates that selection does not affect the histone H1.a polymorphic variants. The stability of histone H1.a during selection might suggest that likely chromatin processes coupled to the selected trait are not linked to the activity of histone H1.a.

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“…Moreover, these cells present interesting specificities such as the expression of an erythroidspecific form of histone linker (H5) that is likely to play a role in the strong chromatin compaction that occurs during the differentiation of these cells (Kowalski and Palyga, 2016).…”

Section: Introductionmentioning

confidence: 99%

Deep proteomic analysis of chicken erythropoiesis

Guillemin

et al. 2018

Preprint

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In contrast to mammalian erythroid cells that lost their nucleus at the end of the differentiation process, circulating chicken erythrocytes, like erythrocytes of most other non-mammalian vertebrates, are nucleated although their nucleus is believed to be transcriptionally silent. This major difference suggests that the erythroid differentiation process is likely to present both similarities and differences in mammals compared to other vertebrates. Since proteins are the major cellular effectors, analysis of the proteome is more prone to reflect true differences than analysis of the pattern of mRNA expression. We have previously reported the evolution of the proteome of human erythroid cells throughout their differentiation process. Here we report the analysis of the proteome of chicken erythroblasts during their terminal differentiation. We used the T2EC cellular model that allows to obtain homogenous populations of immature erythroblasts. Induction of their terminal differentiation led to their maturation and the possibility to obtain cells at different differentiation stages. Mass spectrometry analysis of these cell populations allowed the absolute quantification of 6167 proteins throughout the terminal differentiation process. Beside many proteins with similar expression patterns between chicken and human erythroblasts, like SLC4A1 (Band3), GATA1 or CD44, this analysis also revealed that other important proteins like Kit or other GATA transcription factors exhibit fully different patterns of expression.

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Modulation of chromatin function through linker histone H1 variants

Cited by 20 publications

References 154 publications

Emerging roles of linker histones in regulating chromatin structure and function

Emerging roles of linker histones in regulating chromatin structure and function

Evidence on the stability of histone H1.a polymorphic variants during selection in quail

Deep proteomic analysis of chicken erythropoiesis

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