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Michael Grunstein - One of the best experts on this subject based on the ideXlab platform.
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sir2p and sas2p opposingly regulate acetylation of yeast Histone H4 lysine16 and spreading of heterochromatin
Nature Genetics, 2002Co-Authors: Noriyuki Suka, Kunheng Luo, Michael GrunsteinAbstract:Sir2p and Sas2p opposingly regulate acetylation of yeast Histone H4 lysine16 and spreading of heterochromatin
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sir2p and sas2p opposingly regulate acetylation of yeast Histone H4 lysine16 and spreading of heterochromatin
Nature Genetics, 2002Co-Authors: Noriyuki Suka, Kunheng Luo, Michael GrunsteinAbstract:The Sir3 protein helps form telomeric heterochromatin by interacting with hypoacetylated Histone H4 lysine 16 (H4–Lys16). The molecular nature of the heterochromatin boundary is still unknown. Here we show that the MYST-like acetyltransferase Sas2p is required for the acetylation (Ac) of H4–Lys16 in euchromatin. In a sas2Δ strain or a phenocopy Lys16Arg mutant, Sir3p spreads from roughly 3 kb to roughly 15 kb, causing hypoacetylation and repression of adjacent chromatin. We also found that disruption of Sir3p binding in a deacetylase-deficient Sir 2Δ strain can be suppressed by sas2Δ. These data indicate that opposing effects of Sir2p and Sas2p on acetylation of H4–Lys16 maintain the boundary at telomeric heterochromatin.
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acetylation of the yeast Histone H4 n terminus regulates its binding to heterochromatin protein sir3
Journal of Biological Chemistry, 2002Co-Authors: Andrew A Carmen, Lisa Milne, Michael GrunsteinAbstract:Abstract Heterochromatin at yeast telomeres and silent mating (HM) loci represses adjacent genes and is formed by the binding and spreading of silencinginformation regulators (SIR proteins) along Histones. This involves the interaction between the C terminus of SIR3 and the N terminus of Histone H4. Since H4 is hypoacetylated in heterochromatin we wished to determine whether acetylation is involved in regulating the contacts between SIR3 and H4. Binding of H4 peptide (residues 1–34) acetylated at lysines Lys-5, Lys-8, Lys-12, and Lys-16 to an immobilized SIR3 protein fragment (residues 510–970) was investigated using surface plasmon resonance. We find that acetylation of H4 lysines reduces binding (K a) of H4 to SIR3 in a cumulative manner so that the fully acetylated peptide binding is decreased ∼50-fold relative to unacetylated peptide. Thus, by affecting SIR3-H4 binding, acetylation may regulate the formation of heterochromatin. These data help explain the hypoacetylated state of Histone H4 in heterochromatin of eukaryotes.
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transcriptional repression by ume6 involves deacetylation of lysine 5 of Histone H4 by rpd3
Nature, 1998Co-Authors: Stephen E Rundlett, Andrew A Carmen, Noriyuki Suka, Bryan M Turner, Michael GrunsteinAbstract:Transcriptional repression by UME6 involves deacetylation of lysine 5 of Histone H4 by RPD3
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yeast Histone H4 n terminal sequence is required for promoter activation in vivo
Cell, 1991Co-Authors: Linda K Durrin, R K Mann, Paul S Kayne, Michael GrunsteinAbstract:To search for Histone domains that may regulate transcription in vivo, we made deletions and amino acid substitutions in the Histone N-termini of S. cerevisiae. Histone H4 N-terminal residues 4-23, which include the extremely conserved, reversibly acetylated lysines (at positions 5, 8, 12, and 16), were found to encompass a region required for the activation of the GAL1 promoter. Deletions in the H4 N-terminus reduce GAL1 activation 20-fold. This effect is specific to Histone H4 in that large deletions in the N-termini of H2A, H2B, and H3 do not similarly decrease induction. Activation of the PHO5 promoter is reduced approximately 4- to 5-fold by these H4 deletions. Mutations in Histone H4 acetylation sites and surrounding residues can cause comparable and, in some cases, even greater effects on induction of these two promoters. We postulate that the H4 N-terminus may interact with a component of the transcription initiation complex, allowing nucleosome unfolding and subsequent initiation.
Gonzalo G De Polavieja - One of the best experts on this subject based on the ideXlab platform.
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Histone H4 acetylation regulates behavioral inter individual variability in zebrafish
Genome Biology, 2018Co-Authors: Angel Carlos Roman, Julian Vicentepage, Alfonso Perezescudero, Jose Maria Carvajalgonzalez, Pedro M Fernandezsalguero, Gonzalo G De PolaviejaAbstract:Animals can show very different behaviors even in isogenic populations, but the underlying mechanisms to generate this variability remain elusive. We use the zebrafish (Danio rerio) as a model to test the influence of Histone modifications on behavior. We find that laboratory and isogenic zebrafish larvae show consistent individual behaviors when swimming freely in identical wells or in reaction to stimuli. This behavioral inter-individual variability is reduced when we impair the Histone deacetylation pathway. Individuals with high levels of Histone H4 acetylation, and specifically H4K12, behave similarly to the average of the population, but those with low levels deviate from it. More precisely, we find a set of genomic regions whose Histone H4 acetylation is reduced with the distance between the individual and the average population behavior. We find evidence that this modulation depends on a complex of Yin-yang 1 (YY1) and Histone deacetylase 1 (HDAC1) that binds to and deacetylates these regions. These changes are not only maintained at the transcriptional level but also amplified, as most target regions are located near genes encoding transcription factors. We suggest that stochasticity in the Histone deacetylation pathway participates in the generation of genetic-independent behavioral inter-individual variability.
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Histone H4 acetylation regulates behavioral inter individual variability in zebrafish
bioRxiv, 2017Co-Authors: Angel Carlos Roman, Julian Vicentepage, Alfonso Perezescudero, Jose Maria Carvajalgonzalez, Pedro M Fernandezsalguero, Gonzalo G De PolaviejaAbstract:Animals can show very different behaviors even in isogenic populations, but the underlying mechanisms to generate this variability remain elusive. We found that laboratory and isogenic zebrafish (Danio rerio) larvae showed consistent individual behaviors when swimming freely in identical wells or in reaction to stimuli. We also found that this behavioral inter-individual variability was reduced when we impaired the Histone deacetylation pathway. Individuals with high levels of Histone H4 acetylation, and specifically H4K12, behaved similar to the average of the population, but those with low levels deviated from it. More precisely, we found a set of genomic regions whose Histone H4 acetylation is reduced with the distance between the individual and the average population behavior. We found evidence that this modulation depends on a complex of Yin-yang 1 (YY1) and Histone deacetylase 1 (HDAC1) that binds to and deacetylates these regions. These changes were not only maintained at the transcriptional level but also amplified, as most target regions were located near genes encoding transcription factors. We suggest that stochasticity in the Histone deacetylation pathway participates the generation of genetic-independent behavioral inter-individual variability.
Noriyuki Suka - One of the best experts on this subject based on the ideXlab platform.
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sir2p and sas2p opposingly regulate acetylation of yeast Histone H4 lysine16 and spreading of heterochromatin
Nature Genetics, 2002Co-Authors: Noriyuki Suka, Kunheng Luo, Michael GrunsteinAbstract:The Sir3 protein helps form telomeric heterochromatin by interacting with hypoacetylated Histone H4 lysine 16 (H4–Lys16). The molecular nature of the heterochromatin boundary is still unknown. Here we show that the MYST-like acetyltransferase Sas2p is required for the acetylation (Ac) of H4–Lys16 in euchromatin. In a sas2Δ strain or a phenocopy Lys16Arg mutant, Sir3p spreads from roughly 3 kb to roughly 15 kb, causing hypoacetylation and repression of adjacent chromatin. We also found that disruption of Sir3p binding in a deacetylase-deficient Sir 2Δ strain can be suppressed by sas2Δ. These data indicate that opposing effects of Sir2p and Sas2p on acetylation of H4–Lys16 maintain the boundary at telomeric heterochromatin.
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sir2p and sas2p opposingly regulate acetylation of yeast Histone H4 lysine16 and spreading of heterochromatin
Nature Genetics, 2002Co-Authors: Noriyuki Suka, Kunheng Luo, Michael GrunsteinAbstract:Sir2p and Sas2p opposingly regulate acetylation of yeast Histone H4 lysine16 and spreading of heterochromatin
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transcriptional repression by ume6 involves deacetylation of lysine 5 of Histone H4 by rpd3
Nature, 1998Co-Authors: Stephen E Rundlett, Andrew A Carmen, Noriyuki Suka, Bryan M Turner, Michael GrunsteinAbstract:Transcriptional repression by UME6 involves deacetylation of lysine 5 of Histone H4 by RPD3
Alfonso Perezescudero - One of the best experts on this subject based on the ideXlab platform.
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Histone H4 acetylation regulates behavioral inter individual variability in zebrafish
Genome Biology, 2018Co-Authors: Angel Carlos Roman, Julian Vicentepage, Alfonso Perezescudero, Jose Maria Carvajalgonzalez, Pedro M Fernandezsalguero, Gonzalo G De PolaviejaAbstract:Animals can show very different behaviors even in isogenic populations, but the underlying mechanisms to generate this variability remain elusive. We use the zebrafish (Danio rerio) as a model to test the influence of Histone modifications on behavior. We find that laboratory and isogenic zebrafish larvae show consistent individual behaviors when swimming freely in identical wells or in reaction to stimuli. This behavioral inter-individual variability is reduced when we impair the Histone deacetylation pathway. Individuals with high levels of Histone H4 acetylation, and specifically H4K12, behave similarly to the average of the population, but those with low levels deviate from it. More precisely, we find a set of genomic regions whose Histone H4 acetylation is reduced with the distance between the individual and the average population behavior. We find evidence that this modulation depends on a complex of Yin-yang 1 (YY1) and Histone deacetylase 1 (HDAC1) that binds to and deacetylates these regions. These changes are not only maintained at the transcriptional level but also amplified, as most target regions are located near genes encoding transcription factors. We suggest that stochasticity in the Histone deacetylation pathway participates in the generation of genetic-independent behavioral inter-individual variability.
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Histone H4 acetylation regulates behavioral inter individual variability in zebrafish
bioRxiv, 2017Co-Authors: Angel Carlos Roman, Julian Vicentepage, Alfonso Perezescudero, Jose Maria Carvajalgonzalez, Pedro M Fernandezsalguero, Gonzalo G De PolaviejaAbstract:Animals can show very different behaviors even in isogenic populations, but the underlying mechanisms to generate this variability remain elusive. We found that laboratory and isogenic zebrafish (Danio rerio) larvae showed consistent individual behaviors when swimming freely in identical wells or in reaction to stimuli. We also found that this behavioral inter-individual variability was reduced when we impaired the Histone deacetylation pathway. Individuals with high levels of Histone H4 acetylation, and specifically H4K12, behaved similar to the average of the population, but those with low levels deviated from it. More precisely, we found a set of genomic regions whose Histone H4 acetylation is reduced with the distance between the individual and the average population behavior. We found evidence that this modulation depends on a complex of Yin-yang 1 (YY1) and Histone deacetylase 1 (HDAC1) that binds to and deacetylates these regions. These changes were not only maintained at the transcriptional level but also amplified, as most target regions were located near genes encoding transcription factors. We suggest that stochasticity in the Histone deacetylation pathway participates the generation of genetic-independent behavioral inter-individual variability.
Shelley L Berger - One of the best experts on this subject based on the ideXlab platform.
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Histone H4 lysine 16 acetylation regulates cellular lifespan
Nature, 2009Co-Authors: Weiwei Dang, Jean Dorsey, Shelley L Berger, Kristan K Steffen, Rocco Perry, Brad F Johnson, Ali Shilatifard, Matt Kaeberlein, Brian K KennedyAbstract:Cells undergoing developmental processes are characterized by persistent non-genetic alterations in chromatin, termed epigenetic changes, represented by distinct patterns of DNA methylation and Histone post-translational modifications. Sirtuins, a group of conserved NAD(+)-dependent deacetylases or ADP-ribosyltransferases, promote longevity in diverse organisms; however, their molecular mechanisms in ageing regulation remain poorly understood. Yeast Sir2, the first member of the family to be found, establishes and maintains chromatin silencing by removing Histone H4 lysine 16 acetylation and bringing in other silencing proteins. Here we report an age-associated decrease in Sir2 protein abundance accompanied by an increase in H4 lysine 16 acetylation and loss of Histones at specific subtelomeric regions in replicatively old yeast cells, which results in compromised transcriptional silencing at these loci. Antagonizing activities of Sir2 and Sas2, a Histone acetyltransferase, regulate the replicative lifespan through Histone H4 lysine 16 at subtelomeric regions. This pathway, distinct from existing ageing models for yeast, may represent an evolutionarily conserved function of sirtuins in regulation of replicative ageing by maintenance of intact telomeric chromatin.
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phosphorylation of Histone H4 serine 1 during dna damage requires casein kinase ii in s cerevisiae
Current Biology, 2005Co-Authors: Wang L Cheung, Thanuja Krishnamoorthy, Jean Dorsey, Shelley L Berger, Fiona B Turner, Branden Wolner, Melissa Anne Foley, Craig L Peterson, David C AllisAbstract:Summary Distinct patterns of posttranslational Histone modifications can regulate DNA-templated events such as mitosis, transcription, replication, apoptosis, and DNA damage [1–5], suggesting the presence of a "Histone code" in these nuclear processes [6, 7]. Phosphorylation of Histone H2A S129 at sites of DNA double-strand breaks (DSBs) has been implicated in damage repair in yeast [8, 9]. Here, we describe another phosphorylation event on serine 1 (S1) of Histone H4; this event is also associated with MMS- or phleomycin-induced DSBs but not with UV-induced DNA damage. Chromatin-immunoprecipitation (ChIP) studies of an HO-endonuclease-inducible strain show that S1 phosphorylation is specifically enhanced 20- to 25-fold in nucleosomes proximal to the DSB. In addition, we show that casein kinase II (CK2) can phosphorylate H4 S1 in vitro and that null or temperature-sensitive CK2 yeast mutants are defective for induction of H4 S1 phosphorylation upon DNA damage in vivo. Furthermore, H4 S1 phosphorylation and CK2 play a role in DSB re-joining as indicated by a nonhomologous end-joining (NHEJ) plasmid assay. CK2 has been implicated in regulating a DNA-damage response; our data suggest that Histone H4 S1 is one of its physiological substrates. These data suggest that this modification is a part of the DNA-repair Histone code.