The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
about
yFACT induces global accessibility of nucleosomal DNA without H2A-H2B displacementMechanism of transcription through a nucleosome by RNA polymerase IIEpigenetic inheritance: histone bookmarks across generationsStructure of the Spt16 Middle Domain Reveals Functional Features of the Histone Chaperone FACTStructural basis of histone H2A-H2B recognition by the essential chaperone FACTUniform transitions of the general RNA polymerase II transcription complex.The Modifier of Transcription 1 (Mot1) ATPase and Spt16 Histone Chaperone Co-regulate Transcription through Preinitiation Complex Assembly and Nucleosome Organization.FACT prevents the accumulation of free histones evicted from transcribed chromatin and a subsequent cell cycle delay in G1.Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT ComplexThe histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeatsHistone chaperones link histone nuclear import and chromatin assemblyMutant versions of the S. cerevisiae transcription elongation factor Spt16 define regions of Spt16 that functionally interact with histone H3FACT, the Bur kinase pathway, and the histone co-repressor HirC have overlapping nucleosome-related roles in yeast transcription elongation.Factors that promote H3 chromatin integrity during transcription prevent promiscuous deposition of CENP-A(Cnp1) in fission yeastThe FACT complex interacts with the E3 ubiquitin ligase Psh1 to prevent ectopic localization of CENP-A.The histone chaperone FACT: structural insights and mechanisms for nucleosome reorganization.Histone chaperones in nucleosome assembly and human diseasePhosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements.Genetic interactions between POB3 and the acetylation of newly synthesized histonesHistone chaperones in Arabidopsis and rice: genome-wide identification, phylogeny, architecture and transcriptional regulation.Histone chaperones, histone acetylation, and the fluidity of the chromogenomeLinking DNA replication to heterochromatin silencing and epigenetic inheritanceChromatin and transcription in yeastHistone chaperone FACT coordinates nucleosome interaction through multiple synergistic binding events.Histone Chaperones Spt6 and FACT: Similarities and Differences in Modes of Action at Transcribed GenesIdentification of Mutant Versions of the Spt16 Histone Chaperone That Are Defective for Transcription-Coupled Nucleosome Occupancy in Saccharomyces cerevisiae.FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide MotifsCrystal Structure of Human SSRP1 Middle Domain Reveals a Role in DNA BindingNucleosome assembly and epigenetic inheritanceExpanded binding specificity of the human histone chaperone NASPA nucleosomal region important for ensuring proper interactions between the transcription elongation factor Spt16 and transcribed genes in Saccharomyces cerevisiae.Quantitative Analysis of Dynamic Protein Interactions during Transcription Reveals a Role for Casein Kinase II in Polymerase-associated Factor (PAF) Complex Phosphorylation and Regulation of Histone H2B MonoubiquitylationUncoupling of the patterns of chromatin association of different transcription elongation factors by a histone H3 mutant in Saccharomyces cerevisiae.The FACT histone chaperone guides histone H4 into its nucleosomal conformation in Saccharomyces cerevisiae.A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone VersatilityHistone chaperone networks shaping chromatin function.Chaperoning histones during DNA replication and repair.The histone shuffle: histone chaperones in an energetic dance.The role of FACT in making and breaking nucleosomes.Structure of the human histone chaperone FACT Spt16 N-terminal domain.
P2860
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P2860
The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին 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
The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
@ast
The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
@en
The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
@nl
type
label
The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
@ast
The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
@en
The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
@nl
prefLabel
The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
@ast
The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
@en
The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
@nl
P2093
P2860
P50
P3181
P356
P1476
The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
@en
P2093
Andreas G Ladurner
Tobias Stuwe
Vladimir Rybin
P2860
P304
P3181
P356
10.1073/PNAS.0712293105
P407
P577
2008-07-01T00:00:00Z