Vps75, a new yeast member of the NAP histone chaperone family.
about
Histone H2A/H2B dimer exchange by ATP-dependent chromatin remodeling activities.Histone-modifying enzymes, histone modifications and histone chaperones in nucleosome assembly: Lessons learned from Rtt109 histone acetyltransferasesHistone H2A/H2B chaperones: from molecules to chromatin-based functions in plant growth and developmentMolecular basis for the autoregulation of the protein acetyl transferase Rtt109Structure of Vps75 and implications for histone chaperone functionMolecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75Crystal Structure of Malaria Parasite Nucleosome Assembly Protein: DISTINCT MODES OF PROTEIN LOCALIZATION AND HISTONE RECOGNITIONStructural Analysis of Rtt106p Reveals a DNA Binding Role Required for Heterochromatin SilencingStructure, localization and histone binding properties of nuclear-associated nucleosome assembly protein from Plasmodium falciparumStructure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone AcetylationThe histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexesHistone chaperone specificity in Rtt109 activation.Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109.GTP-dependent binding and nuclear transport of RNA polymerase II by Npa3 proteinPhosphorylation by casein kinase 2 regulates Nap1 localization and function.Hst3 and Hst4 histone deacetylases regulate replicative lifespan by preventing genome instability in Saccharomyces cerevisiae.Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongationInteraction with the histone chaperone Vps75 promotes nuclear localization and HAT activity of Rtt109 in vivo.HPC2 and ubinuclein define a novel family of histone chaperones conserved throughout eukaryotes.Identification of distinct SET/TAF-Ibeta domains required for core histone binding and quantitative characterisation of the interactionHistone chaperones in nucleosome assembly and human diseaseNuclear Hat1p complex (NuB4) components participate in DNA repair-linked chromatin reassembly.The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformationHistone chaperones, histone acetylation, and the fluidity of the chromogenomeRNA secondary structure mediates alternative 3'ss selection in Saccharomyces cerevisiaeRegulation of rtt107 recruitment to stalled DNA replication forks by the cullin rtt101 and the rtt109 acetyltransferase.The carboxyl terminus of Rtt109 functions in chaperone control of histone acetylationPlasticity and epigenetic inheritance of centromere-specific histone H3 (CENP-A)-containing nucleosome positioning in the fission yeastHistone chaperones: an escort network regulating histone traffic.Chromosome Duplication in Saccharomyces cerevisiae.Coordinated Action of Nap1 and RSC in Disassembly of Tandem NucleosomesHistone chaperone networks shaping chromatin function.The histone shuffle: histone chaperones in an energetic dance.Regulation of histone gene transcription in yeast.An rtt109-independent role for vps75 in transcription-associated nucleosome dynamics.Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading.The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.Characterization of the Pneumocystis carinii histone acetyltransferase chaperone proteins PcAsf1 and PcVps75.Homocitrate synthase connects amino acid metabolism to chromatin functions through Esa1 and DNA damage.Kinetic mechanism of the Rtt109-Vps75 histone acetyltransferase-chaperone complex.
P2860
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P2860
Vps75, a new yeast member of the NAP histone chaperone family.
description
2007 nî lūn-bûn
@nan
2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Vps75, a new yeast member of the NAP histone chaperone family.
@ast
Vps75, a new yeast member of the NAP histone chaperone family.
@en
Vps75, a new yeast member of the NAP histone chaperone family.
@nl
type
label
Vps75, a new yeast member of the NAP histone chaperone family.
@ast
Vps75, a new yeast member of the NAP histone chaperone family.
@en
Vps75, a new yeast member of the NAP histone chaperone family.
@nl
prefLabel
Vps75, a new yeast member of the NAP histone chaperone family.
@ast
Vps75, a new yeast member of the NAP histone chaperone family.
@en
Vps75, a new yeast member of the NAP histone chaperone family.
@nl
P2860
P3181
P356
P1476
Vps75, a new yeast member of the NAP histone chaperone family.
@en
P2860
P304
P3181
P356
10.1074/JBC.C700012200
P407
P577
2007-04-27T00:00:00Z