Histone acetylation and deacetylation in yeast

By S. Kurdistani, M. Grunstein. Nature reviews. Molecular cell biology, 2003

727 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/aa0306bf51a57c07ea292da9656b6d504465d7fb

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Citations in the corpus

Extensive Association of Functionally and Cytotopically Related mRNAs with Puf Family RNA-Binding Proteins in Yeast (2004, background): “Puf5p was associated with all of the histone deacetylases (HDACs) that act on histones located around coding sequences—Sin3p (a class I HDAC), Hda1p (a class II HDAC), and both components of the Set3C complex (Hst1p and Snt1p) ( Kurdistani and Grunstein 2003 ).”
The diverse functions of histone lysine methylation (2005, background): “From the time that the hypothesis was first proposed, the existence of a histone code has been questioned 24 .”
Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. (2004, background): “Histone acetylation is often correlated with gene activation, suggesting that histone deacetylases act to silence genes, but genetic experiments in Drosophila and the yeast Saccharomyces cerevisiae have indicated that deacetylase activity can contribute to gene activation as well.(1) – 4 Acetylation”
Gardening the genome: DNA methylation in Arabidopsis thaliana (2005, neutral): “cerevisiae , which function in transcriptional silencin”
The many roles of histone deacetylases in development and physiology: implications for disease and therapy (2009, background): “The class I HDAC family consists of HDAC1, 2, 3 and 8, which share homology with Rpd3 — a founding member from budding yeas”
Histone acetylation by Trrap–Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks (2006, background): “The role of chromatin acetylation by histone acetyltransferase (HAT) complexes in transcriptional regulation is well establishe”
Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription. (2005, background): “The second recruitment *Correspondence: jlw@stowers-institute.org mechanism involves Rpd3 suppression of genome wide histone acetylation levels that is independent of sequence-specific repressor proteins (Kurdistani and Grunstein, 2003).”
Mapping global histone acetylation patterns to gene expression. (2004, background): “…acetylation sites (HDAC) as coregulators in transcription, DNA replica- for recruitment of transcription-related complexes for tion, and DNA repair (Kurdistani and Grunstein, 2003). activation specifically of the human IFN- gene (Agalioti The sites of acetylation include at least four highly con-…”
The nucleosome: from genomic organization to genomic regulation. (2004, background): “The structure of the HAT domain shows a central conserved core unit that is important forverse roles in the regulation of the nucleosome (for review see, Kurdistani and Grunstein, 2003).”
The NAD+-Dependent Deacetylase SIRT1 Modulates CLOCK-Mediated Chromatin Remodeling and Circadian Control (2008, neutral): “Unique combinations of these modifications, for which the ‘‘histone code’’ hypothesis has been formulated (Strahl and Allis, 2000), induce conformational changes of chromatin, rendering it permissive to transcription, silencing, DNA replication, and repair (Cheung et al., 2000a; Kouzarides, 2007; Ku”
Histone deacetylase 5 epigenetically controls behavioral adaptations to chronic emotional stimuli. (2007, neutral): “There are three distinct classes of HDACs, classes I, II, and III, based on their homology to the yeast genes rpd3, hda1, and sir2, respectively (Kurdistani and Grunstein, 2003).”
A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. (2004, background): “Indeed, the distinctions between di- and trimethylation of H3-K4 (Santos-Rosa et al. 2002) or of H3-K9 residues (Czermin et al. 2002; Kuzmichev et al. 2002; Tamaru et al. 2003) have been shown to be relevant for transcriptional regulation or Polycomb-mediated gene silencing.”
Structures of RNA polymerase II complexes with Bye1, a chromatin-binding PHF3/DIDO homologue (2013, neutral): “P82 H4 11–27 Ac-GKGGAKRHRK(Me3)VLRDNIQ-Peg-Biot H4K20me3 P83 H4 11–27 Ac-GKGGAKRHRK(Me2)VLRDNIQ-Peg-Biot H4K20me2 P84 H4 11–27 Ac-GKGGAKRHRK(Me)VLRDNIQ-Peg-Biot H4K20me1 P85 H4 11–27 Ac-GK(Ac)GGAK(Ac)RHRK(Me3)VLRDNIQ-Peg-Biot H4K12ac + K16ac + K20me3 P86 H4 11–27 Ac-GK(Ac)GGAK(Ac)RHRK(Me2)VLRDNIQ-Pe”