Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
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Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transductionA human homologue of yeast anti-silencing factor has histone chaperone activityA cooperative activation loop among SWI/SNF, gamma-H2AX and H3 acetylation for DNA double-strand break repairAnd-1 is required for the stability of histone acetyltransferase Gcn5Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo.Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family membersFunctional proteomics establishes the interaction of SIRT7 with chromatin remodeling complexes and expands its role in regulation of RNA polymerase I transcriptionComposition of the SAGA complex in plants and its role in controlling gene expression in response to abiotic stressesKATs in cancer: functions and therapiesCrystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivatorDimeric structure of p300/CBP associated factorSet2 methylation of histone H3 lysine 36 suppresses histone exchange on transcribed genes.Global assessment of combinatorial post-translational modification of core histones in yeast using contemporary mass spectrometry. LYS4 trimethylation correlates with degree of acetylation on the same H3 tail.HAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4.Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation.The Rpb9 subunit of RNA polymerase II binds transcription factor TFIIE and interferes with the SAGA and elongator histone acetyltransferases.Tip60 acetylates six lysines of a specific class in core histones in vitroThe histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, TatNovel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60Nerve growth factor receptor signaling induces histone acetyltransferase domain-dependent nuclear translocation of p300/CREB-binding protein-associated factor and hGCN5 acetyltransferasesHow chromatin-binding modules interpret histone modifications: lessons from professional pocket pickersMethylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in TetrahymenaAdenovirus E1A requires the yeast SAGA histone acetyltransferase complex and associates with SAGA components Gcn5 and Tra1.Interaction with the histone chaperone Vps75 promotes nuclear localization and HAT activity of Rtt109 in vivo.Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification.Mutational analysis of H3 and H4 N termini reveals distinct roles in nuclear import.Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activationFrom human monocytes to genome-wide binding sites--a protocol for small amounts of blood: monocyte isolation/ChIP-protocol/library amplification/genome wide computational data analysis.The regulation of gene activity by histones and the histone deacetylase RPD3.Signaling to chromatin through histone modifications: how clear is the signal?TBP-associated factors in the PCAF histone acetylase complex.Structure of the yeast histone acetyltransferase Hat1: insights into substrate specificity and implications for the Gcn5-related N-acetyltransferase superfamily.The SAGA of Spt proteins and transcriptional analysis in yeast: past, present, and future.Proliferating cell nuclear antigen (PCNA) is required for cell cycle-regulated silent chromatin on replicated and nonreplicated genes.Investigation of the acetylation mechanism by GCN5 histone acetyltransferase.Protein modules that manipulate histone tails for chromatin regulation.An embarrassment of niches: the many covalent modifications of histones in transcriptional regulation.Multiple histone methyl and acetyltransferase complex components bind the HLA-DRA gene.Cell cycle-regulated oscillator coordinates core histone gene transcription through histone acetylation.A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response.
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Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature у вересні 1996
@uk
name
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
@en
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
@nl
type
label
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
@en
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
@nl
prefLabel
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
@en
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
@nl
P2093
P356
P1433
P1476
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
@en
P2093
Brownell JE
Edmondson DG
Ranalli TA
P2888
P304
P356
10.1038/383269A0
P407
P577
1996-09-01T00:00:00Z
P6179
1024313273