Eaf1 is the platform for NuA4 molecular assembly that evolutionarily links chromatin acetylation to ATP-dependent exchange of histone H2A variants.
about
Epigenetic modifications in double-strand break DNA damage signaling and repairN terminus of Swr1 binds to histone H2AZ and provides a platform for subunit assembly in the chromatin remodeling complexNuA4 lysine acetyltransferase Esa1 is targeted to coding regions and stimulates transcription elongation with Gcn5.Mutational analysis of the C-terminal FATC domain of Saccharomyces cerevisiae Tra1.Multiple histone modifications in euchromatin promote heterochromatin formation by redundant mechanisms in Saccharomyces cerevisiae.NuA4-dependent acetylation of nucleosomal histones H4 and H2A directly stimulates incorporation of H2A.Z by the SWR1 complex.Eaf5/7/3 form a functionally independent NuA4 submodule linked to RNA polymerase II-coupled nucleosome recycling.Histone H4 lysine 12 acetylation regulates telomeric heterochromatin plasticity in Saccharomyces cerevisiaeDeposition of histone variant H2A.Z within gene bodies regulates responsive genesThe multi-copy mouse gene Sycp3-like Y-linked (Sly) encodes an abundant spermatid protein that interacts with a histone acetyltransferase and an acrosomal proteinAnalysis of Myc-induced histone modifications on target chromatin.Chapter 5. Nuclear actin-related proteins in epigenetic control.SWR1 complex poises heterochromatin boundaries for antisilencing activity propagation.Distinct configurations of protein complexes and biochemical pathways revealed by epistatic interaction network motifs.Regulation of septin dynamics by the Saccharomyces cerevisiae lysine acetyltransferase NuA4SETD6 controls the expression of estrogen-responsive genes and proliferation of breast carcinoma cells.NuA4 links methylation of histone H3 lysines 4 and 36 to acetylation of histones H4 and H3A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation.YEATS domain proteins: a diverse family with many links to chromatin modification and transcription.AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex.The NuA4 complex promotes translesion synthesis (TLS)-mediated DNA damage tolerance.Structure and nucleosome interaction of the yeast NuA4 and Piccolo-NuA4 histone acetyltransferase complexes.Overlapping Functions between SWR1 Deletion and H3K56 Acetylation in Candida albicans.The double-bromodomain proteins Bdf1 and Bdf2 modulate chromatin structure to regulate S-phase stress response in Schizosaccharomyces pombeCharacterization of MRFAP1 turnover and interactions downstream of the NEDD8 pathway.Eaf1p Is Required for Recruitment of NuA4 in Targeting TFIID to the Promoters of the Ribosomal Protein Genes for Transcriptional Initiation In Vivo.Genetic evidence links the ASTRA protein chaperone component Tti2 to the SAGA transcription factor Tra1.The Eaf3/5/7 Subcomplex Stimulates NuA4 Interaction with Methylated Histone H3 Lys-36 and RNA Polymerase II.H2A.Z.2.2 is an alternatively spliced histone H2A.Z variant that causes severe nucleosome destabilizationAtaxia telangiectasia mutated (ATM) interacts with p400 ATPase for an efficient DNA damage response.Lysine acetyltransferase NuA4 and acetyl-CoA regulate glucose-deprived stress granule formation in Saccharomyces cerevisiae.A Genome-Wide Screen with Nicotinamide to Identify Sirtuin-Dependent Pathways in Saccharomyces cerevisiae.Schizosaccharomyces pombe histone acetyltransferase Mst1 (KAT5) is an essential protein required for damage response and chromosome segregationRegulation of Antisense Transcription by NuA4 Histone Acetyltransferase and Other Chromatin Regulatory FactorsA gene ontology inferred from molecular networks.Roles for the Histone Modifying and Exchange Complex NuA4 in Cell Cycle Progression in Drosophila melanogaster.Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis.Cooperative action of TIP48 and TIP49 in H2A.Z exchange catalyzed by acetylation of nucleosomal H2A.Connection between histone H2A variants and chromatin remodeling complexes.Histone acetylation: truth of consequences?
P2860
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P2860
Eaf1 is the platform for NuA4 molecular assembly that evolutionarily links chromatin acetylation to ATP-dependent exchange of histone H2A variants.
description
2008 nî lūn-bûn
@nan
2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Eaf1 is the platform for NuA4 ...... hange of histone H2A variants.
@ast
Eaf1 is the platform for NuA4 ...... hange of histone H2A variants.
@en
Eaf1 is the platform for NuA4 ...... hange of histone H2A variants.
@nl
type
label
Eaf1 is the platform for NuA4 ...... hange of histone H2A variants.
@ast
Eaf1 is the platform for NuA4 ...... hange of histone H2A variants.
@en
Eaf1 is the platform for NuA4 ...... hange of histone H2A variants.
@nl
prefLabel
Eaf1 is the platform for NuA4 ...... hange of histone H2A variants.
@ast
Eaf1 is the platform for NuA4 ...... hange of histone H2A variants.
@en
Eaf1 is the platform for NuA4 ...... hange of histone H2A variants.
@nl
P2093
P2860
P3181
P356
P1476
Eaf1 is the platform for NuA4 ...... hange of histone H2A variants.
@en
P2093
Amine Nourani
Andréanne Auger
Dominique Cronier
Jacques Côté
Luc Galarneau
Mohammed Altaf
Rhea T Utley
Stéphane Allard
Yannick Doyon
P2860
P304
P3181
P356
10.1128/MCB.01755-07
P407
P577
2008-04-01T00:00:00Z