Redundant roles for the TFIID and SAGA complexes in global transcription. - Wikidata - awgldk - TriplyDB

Redundant roles for the TFIID and SAGA complexes in global transcription.

Redundant roles for the TFIID and SAGA complexes in global transcription.

http://www.wikidata.org/entity/Q38311191

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Selectivity of chromatin-remodelling cofactors for ligand-activated transcription Structural analysis and dimerization potential of the human TAF5 subunit of TFIID TAF7: a possible transcription initiation check-point regulator TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping roles with TAF9 Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.TFIID and Spt-Ada-Gcn5-acetyltransferase functions probed by genome-wide synthetic genetic array analysis using a Saccharomyces cerevisiae taf9-ts allele Analysis of Gal4-directed transcription activation using Tra1 mutants selectively defective for interaction with Gal4 Minimal components of the RNA polymerase II transcription apparatus determine the consensus TATA box The new core promoter element XCPE1 (X Core Promoter Element 1) directs activator-, mediator-, and TATA-binding protein-dependent but TFIID-independent RNA polymerase II transcription from TATA-less promoters A multiplicity of coactivators is required by Gcn4p at individual promoters in vivo Progress in the application of DNA microarrays Composition of the SAGA complex in plants and its role in controlling gene expression in response to abiotic stresses SGF29 and Sry pathway in hepatocarcinogenesis Sumoylation and transcription regulation at nuclear pores Crystal structure of a subcomplex of human transcription factor TFIID formed by TATA binding protein-associated factors hTAF4 (hTAF(II)135) and hTAF12 (hTAF(II)20)Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D Artificial recruitment of certain Mediator components affects requirement of basal transcription factor IIE.Use of a genetically introduced cross-linker to identify interaction sites of acidic activators within native transcription factor IID and SAGA.Sgf29p facilitates the recruitment of TATA box binding protein but does not alter SAGA's global structural integrity in vivo.Differential requirement of SAGA components for recruitment of TATA-box-binding protein to promoters in vivo.Cooperative action of NC2 and Mot1p to regulate TATA-binding protein function across the genome Rvb1p and Rvb2p are essential components of a chromatin remodeling complex that regulates transcription of over 5% of yeast genes.Mutations in the histone fold domain of the TAF12 gene show synthetic lethality with the TAF1 gene lacking the TAF N-terminal domain (TAND) by different mechanisms from those in the SPT15 gene encoding the TATA box-binding protein (TBP)An array of coactivators is required for optimal recruitment of TATA binding protein and RNA polymerase II by promoter-bound Gcn4p.TATA-binding protein variants that bypass the requirement for Mot1 in vivo Positive and negative functions of the SAGA complex mediated through interaction of Spt8 with TBP and the N-terminal domain of TFIIA.Global regulation by the yeast Spt10 protein is mediated through chromatin structure and the histone upstream activating sequence elements.The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway.SAGA-associated Sgf73p facilitates formation of the preinitiation complex assembly at the promoters either in a HAT-dependent or independent manner in vivo.Analysis of Spt7 function in the Saccharomyces cerevisiae SAGA coactivator complex.SAGA binds TBP via its Spt8 subunit in competition with DNA: implications for TBP recruitment.In vivo target of a transcriptional activator revealed by fluorescence resonance energy transfer Pho91 Is a vacuolar phosphate transporter that regulates phosphate and polyphosphate metabolism in Saccharomyces cerevisiae.The N-terminus and Tudor domains of Sgf29 are important for its heterochromatin boundary formation function.Yeast Sgf73/Ataxin-7 serves to anchor the deubiquitination module into both SAGA and Slik(SALSA) HAT complexes.The TAF9 C-terminal conserved region domain is required for SAGA and TFIID promoter occupancy to promote transcriptional activation.Distinct mutations in yeast TAF(II)25 differentially affect the composition of TFIID and SAGA complexes as well as global gene expression patterns.Fluorescence-based analyses of the effects of full-length recombinant TAF130p on the interaction of TATA box-binding protein with TATA box DNA.The Saccharomyces cerevisiae Srb8-Srb11 complex functions with the SAGA complex during Gal4-activated transcription.Cluster analysis of mass spectrometry data reveals a novel component of SAGA

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Redundant roles for the TFIID and SAGA complexes in global transcription.

http://www.wikidata.org/entity/Q38311191

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2000 nî lūn-bûn

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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2000年论文

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2000年论文

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name

Redundant roles for the TFIID and SAGA complexes in global transcription.

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type

label

Redundant roles for the TFIID and SAGA complexes in global transcription.

@en

prefLabel

Redundant roles for the TFIID and SAGA complexes in global transcription.

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Redundant roles for the TFIID and SAGA complexes in global transcription.

@en

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Causton HC

http://www.w3.org/2001/XMLSchema#string

Green MR

http://www.w3.org/2001/XMLSchema#string

Hannett N

http://www.w3.org/2001/XMLSchema#string

Holstege FC

http://www.w3.org/2001/XMLSchema#string

Jennings EG

http://www.w3.org/2001/XMLSchema#string

Lee TI

http://www.w3.org/2001/XMLSchema#string

Shen WC

http://www.w3.org/2001/XMLSchema#string

Winston F

http://www.w3.org/2001/XMLSchema#string

Young RA

http://www.w3.org/2001/XMLSchema#string

P2860

The TAF(II)250 subunit of TFIID has histone acetyltransferase activity

Structural similarity between TAFs and the heterotetrameric core of the histone octamer

The histone H3-like TAF is broadly required for transcription in yeast.

Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction.

The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae.

Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex.

A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation.

Yeast TAF(II)145 functions as a core promoter selectivity factor, not a general coactivator.

Yeast TAF(II)145 required for transcription of G1/S cyclin genes and regulated by the cellular growth state.

ADA1, a novel component of the ADA/GCN5 complex, has broader effects than GCN5, ADA2, or ADA3.

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701-704

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10.1038/35015104

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6787

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405

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2000-06-01T00:00:00Z

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232803458

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1032268438

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