N- and C-terminal Domains Determine Differential Nucleosomal Binding Geometry and Affinity of Linker Histone Isotypes H10 and H1c

Vyas, Payal; Brown, David T.

doi:10.1074/jbc.m111.312819

Cited by 51 publications

(47 citation statements)

References 54 publications

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“…Modeling suggests that a highly charged CTD compacts chromatin more effectively, resulting in silencing, whereas less-charged CTDs promote a chromatin folding in which the genome is more accessible (42). The N terminus, which is also unstructured, affects positioning and DNA binding affinity (43,44). While specific H1 binding modes may be FIG 3 Domain organization of H1, Hho1p, and HMO1.…”

Section: Linker Histonesmentioning

confidence: 99%

Yeast HMO1: Linker Histone Reinvented

Panday

Grove

2017

Microbiol Mol Biol Rev

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SUMMARY Eukaryotic genomes are packaged in chromatin. The higher-order organization of nucleosome core particles is controlled by the association of the intervening linker DNA with either the linker histone H1 or high mobility group box (HMGB) proteins. While H1 is thought to stabilize the nucleosome by preventing DNA unwrapping, the DNA bending imposed by HMGB may propagate to the nucleosome to destabilize chromatin. For metazoan H1, chromatin compaction requires its lysine-rich C-terminal domain, a domain that is buried between globular domains in the previously characterized yeast Saccharomyces cerevisiae linker histone Hho1p. Here, we discuss the functions of S. cerevisiae HMO1, an HMGB family protein unique in containing a terminal lysine-rich domain and in stabilizing genomic DNA. On ribosomal DNA (rDNA) and genes encoding ribosomal proteins, HMO1 appears to exert its role primarily by stabilizing nucleosome-free regions or “fragile” nucleosomes. During replication, HMO1 likewise appears to ensure low nucleosome density at DNA junctions associated with the DNA damage response or the need for topoisomerases to resolve catenanes. Notably, HMO1 shares with the mammalian linker histone H1 the ability to stabilize chromatin, as evidenced by the absence of HMO1 creating a more dynamic chromatin environment that is more sensitive to nuclease digestion and in which chromatin-remodeling events associated with DNA double-strand break repair occur faster; such chromatin stabilization requires the lysine-rich extension of HMO1. Thus, HMO1 appears to have evolved a unique linker histone-like function involving the ability to stabilize both conventional nucleosome arrays as well as DNA regions characterized by low nucleosome density or the presence of noncanonical nucleosomes.

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Section: Linker Histonesmentioning

confidence: 99%

Yeast HMO1: Linker Histone Reinvented

Panday

Grove

2017

Microbiol Mol Biol Rev

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“…The function of CTD in condensing chromatin is related to its length, the density of basic residues, the number of S/TPXK sites and its specific amino acid composition, as well as the intrinsic protein disorder in the CTD [53, 68]. The N-terminal tail appears to be dispensable for chromatin binding, nevertheless, its deletion or swapping between different H1 variants alters the binding affinity of the respective H1 variant for chromatin [47, 48, 50]. Not surprisingly, different H1 variants also display differential in vivo binding dynamics in oocytes and during ES cell nuclear transfer [69].…”

Section: Overview: Histone H1 and Its Variants In Mammalsmentioning

confidence: 99%

Role of H1 linker histones in mammalian development and stem cell differentiation

Pan

Fan

2016

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

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H1 linker histones are key chromatin architectural proteins facilitating the formation of higher order chromatin structures. The H1 family constitutes the most heterogeneous group of histone proteins, with eleven non-allelic H1 variants in mammals. H1 variants differ in their biochemical properties and exhibit significant sequence divergence from one another, yet most of them are highly conserved during evolution from mouse to human. H1 variants are differentially regulated during development and their cellular compositions undergo dramatic changes in embryogenesis, gametogenesis, tissue maturation and cellular differentiation. As a group, H1 histones are essential for mouse development and proper stem cell differentiation. Here we summarize our current knowledge on the expression and functions of H1 variants in mammalian development and stem cell differentiation. Their diversity, sequence conservation, complex expression and distinct functions suggest that H1s mediate chromatin reprogramming and contribute to the large variations and complexity of chromatin structure and gene expression in the mammalian genome.

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“…However, due to a substantial content of positively charged amino acids, the C-terminal domain of mutated histone H1.0 mediates the formation of a highly compacted chromatin state and the inhibition of DNA replication [14]. These findings together with other data stressing the individual impact of histone H1.0 globular [48] and terminal [13] domain on nucleosome surface interaction and chromatin binding affinity, respectively, indicate that histone H1.0 may evoke a characteristic chromatin environment by differential interactions with both DNA and potential partner proteins. Mutated histone H1.0 analyzed by photobleaching microscopy revealed two clusters of amino acid residues forming DNA-binding sites within the globular domain.…”

Section: Introductionmentioning

confidence: 99%

Nuclear and nucleolar activity of linker histone variant H1.0

Kowalski

2016

Cell Mol Biol Lett

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Histone H1.0 belongs to the class of linker histones (H1), although it is substantially distinct from other histone H1 family members. The differences can be observed in the chromosomal location and organization of the histone H1.0 encoding gene, as well as in the length and composition of its amino acid chain. Whereas somatic (H1.1–H1.5) histone H1 variants are synthesized in the cell cycle S-phase, histone H1.0 is synthesized throughout the cell cycle. By replacing somatic H1 variants during cell maturation, histone H1.0 is gradually deposited in low dividing cells and achieves the highest level of expression in the terminally differentiated cells. Compared to other differentiation-specific H1 histone (H5) characteristic for unique tissue and organisms, the distribution of histone H1.0 remains non-specific. Classic investigations emphasize that histone H1.0 is engaged in the organization of nuclear chromatin accounting for formation and maintenance of its nucleosomal and higher-order structure, and thus influences gene expression. However, the recent data confirmed histone H1.0 peculiar localization in the nucleolus and unexpectedly revealed its potential for regulation of nucleolar, RNA-dependent, activity via interaction with other proteins. According to such findings, histone H1.0 participates in the formation of gene-coded information through its control at both transcriptional and translational levels. In order to reappraise the biological significance of histone H1.0, both aspects of its activity are presented in this review.

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N- and C-terminal Domains Determine Differential Nucleosomal Binding Geometry and Affinity of Linker Histone Isotypes H10 and H1c

Cited by 51 publications

References 54 publications

Yeast HMO1: Linker Histone Reinvented

Yeast HMO1: Linker Histone Reinvented

Role of H1 linker histones in mammalian development and stem cell differentiation

Nuclear and nucleolar activity of linker histone variant H1.0

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