Histone H1 of <i>Saccharomyces cerevisiae</i> Inhibits Transcriptional Silencing

Veron, Marie; Zou, Yanfei; Yu, Qun; Bi, Xin; Selmi, Abdelkader; Gilson, Éric; Defossez, Pierre‐Antoine

doi:10.1534/genetics.105.050195

Cited by 21 publications

(30 citation statements)

References 29 publications

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“…A general role for Hho1p in the formation of DNA loops and for DNA compaction during stationary phase was also reported (62,63). In contrast, Hho1p has also been demonstrated to prevent the establishment of silent chromatin, perhaps by modifying the barriers that separate transcriptionally active chromatin from heterochromatin (57,(63)(64)(65). Thus, both H1 and Hho1p have been implicated in long-range DNA looping and DNA compaction; however, the molecular mechanisms by which these proteins exert such functions are likely to differ.…”

Section: Figmentioning

confidence: 84%

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: Figmentioning

confidence: 84%

Yeast HMO1: Linker Histone Reinvented

Panday

Grove

2017

Microbiol Mol Biol Rev

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“…Reactions were stopped by boiling mixtures for 5 min in an equal volume of 2ϫ SDS-PAGE buffer. Reaction products were subsequently separated by 15% SDS-PAGE, transferred onto nitrocellulose paper, and immunoblotted with antibodies as indicated in the figures and/or figure legends at the following concentrations: HIS probe (1:4,000; Santa Cruz), anti-H3K9ac (1:4,000; Abcam), anti-H3K56ac (1:4,000; a gift from J. Recht), anti-H3K56ac (1: 2,500; Upstate), anti-H3K12ac (1:4,000; Active Motive), and antiHho1(1:2,000) (a gift from Pierre Defossez [50]). Protein concentrations were assessed as required using NanoDrop 2000c (Thermo Scientific) using the Protein A280 application.…”

Section: Methodsmentioning

confidence: 99%

The Carboxyl Terminus of Rtt109 Functions in Chaperone Control of Histone Acetylation

et al. 2013

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e Rtt109 is a fungal histone acetyltransferase (HAT) that catalyzes histone H3 acetylation functionally associated with chromatin assembly. Rtt109-mediated H3 acetylation involves two histone chaperones, Asf1 and Vps75. In vivo, Rtt109 requires both chaperones for histone H3 lysine 9 acetylation (H3K9ac) but only Asf1 for full H3K56ac. In vitro, Rtt109-Vps75 catalyzes both H3K9ac and H3K56ac, whereas Rtt109-Asf1 catalyzes only H3K56ac. In this study, we extend the in vitro chaperone-associated substrate specificity of Rtt109 by showing that it acetylates vertebrate linker histone in the presence of Vps75 but not Asf1. In addition, we demonstrate that in Saccharomyces cerevisiae a short basic sequence at the carboxyl terminus of Rtt109 (Rtt109C) is required for H3K9ac in vivo. Furthermore, through in vitro and in vivo studies, we demonstrate that Rtt109C is required for optimal H3K56ac by the HAT in the presence of full-length Asf1. When Rtt109C is absent, Vps75 becomes important for H3K56ac by Rtt109 in vivo. In addition, we show that lysine 290 (K290) in Rtt109 is required in vivo for Vps75 to enhance the activity of the HAT. This is the first in vivo evidence for a role for Vps75 in H3K56ac. Taken together, our results contribute to a better understanding of chaperone control of Rtt109-mediated H3 acetylation.

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“…Microarray analyses have revealed that expression of very few genes is altered in cells lacking HHO1 (Freidkin and Katcoff, 2001; Hellauer et al ., 2001). Moreover, defects in gene silencing at the silent mating‐type loci or telomeres, phenotypes often associated with mutations that alter chromatin function, have not been observed in cells lacking histone H1 (Escher and Schaffner, 1997; Patterton et al ., 1998; Veron et al ., 2006). Evidence supporting a role for S. cerevisiae histone H1 in chromatin function has been provided by two reports.…”

Section: Introductionmentioning

confidence: 99%

Linker histone H1 represses recombination at the ribosomal DNA locus in the budding yeast Saccharomyces cerevisiae

Mueller

Elfline

et al. 2008

Molecular Microbiology

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SummarySeveral epigenetic phenomena occur at ribosomal DNA loci in eukaryotic cells, including the silencing of Pol I and Pol II transcribed genes, silencing of replication origins and repression of recombination. In Saccharomyces cerevisiae, studies focusing on the silencing of Pol II transcription and genetic recombination at the ribosomal DNA locus (rDNA) have provided insight into the mechanisms through which chromatin and chromatin-associated factors regulate gene expression and chromosome stability. The core histones, H2A, H2B, H3 and H4, the fundamental building blocks of chromatin, have been shown to regulate silent chromatin at the rDNA; however, the function of the linker histone H1 has not been well characterized. Here, we show that S. cerevisiae histone H1 represses recombination at the rDNA without affecting Pol II gene silencing. The most highly studied repressor of recombination at the rDNA is the Silent information regulator protein Sir2. We find that cells lacking histone H1 do not exhibit a premature-ageing phenotype nor do they accumulate the rDNA recombination intermediates and products that are found in cells lacking Sir2. These results suggest that histone H1 represses recombination at the rDNA by a mechanism that is independent of the recombination pathways regulated by Sir2.

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Histone H1 of Saccharomyces cerevisiae Inhibits Transcriptional Silencing

Cited by 21 publications

References 29 publications

Yeast HMO1: Linker Histone Reinvented

Yeast HMO1: Linker Histone Reinvented

The Carboxyl Terminus of Rtt109 Functions in Chaperone Control of Histone Acetylation

Linker histone H1 represses recombination at the ribosomal DNA locus in the budding yeast Saccharomyces cerevisiae

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