Identification of human TFIID components and direct interaction between a 250-kDa polypeptide and the TATA box-binding protein (TFIID tau).
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The crystal structure of CCG1/TAF(II)250-interacting factor B (CIB)Structure and function of a human transcription factor TFIIIB subunit that is evolutionarily conserved and contains both TFIIB- and high-mobility-group protein 2-related domainsSpecific interactions and potential functions of human TAFII100Cloning and expression of Drosophila TAFII60 and human TAFII70 reveal conserved interactions with other subunits of TFIIDDSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologsEvolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factorsIdentification and characterization of CIA/ASF1 as an interactor of bromodomains associated with TFIIDStudies of nematode TFIIE function reveal a link between Ser-5 phosphorylation of RNA polymerase II and the transition from transcription initiation to elongationThe carboxy terminus of the small subunit of TFIIE regulates the transition from transcription initiation to elongation by RNA polymerase IITranscription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesisCharacterization of the transcription activation function and the DNA binding domain of transcriptional enhancer factor-1Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formationEvidence that TAF-TATA box-binding protein interactions are required for activated transcription in mammalian cells.The major transcriptional transactivation domain of simian virus 40 large T antigen associates nonconcurrently with multiple components of the transcriptional preinitiation complexTIPT2 and geminin interact with basal transcription factors to synergize in transcriptional regulation.Promoting developmental transcription.Core promoter-specific function of a mutant transcription factor TFIID defective in TATA-box bindingThe yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding proteinUnique TATA-binding protein-containing complexes and cofactors involved in transcription by RNA polymerases II and III.Interaction between the N-terminal domain of the 230-kDa subunit and the TATA box-binding subunit of TFIID negatively regulates TATA-box bindingAnalysis of the role of TFIIE in basal transcription and TFIIH-mediated carboxy-terminal domain phosphorylation through structure-function studies of TFIIE-alpha.The yeast TATA-binding protein (TBP) core domain assembles with human TBP-associated factors into a functional TFIID complexRNA polymerase II cofactor PC2 facilitates activation of transcription by GAL4-AH in vitro.Molecular cloning, expression, and characterization of the Drosophila 85-kilodalton TFIID subunitRemoving the vertebrate-specific TBP N terminus disrupts placental beta2m-dependent interactions with the maternal immune systemTATA-binding protein-associated factor(s) in TFIID function through the initiator to direct basal transcription from a TATA-less class II promoter.Structure-function analysis of TAF130: identification and characterization of a high-affinity TATA-binding protein interaction domain in the N terminus of yeast TAF(II)130A C-terminal domain in FosB, absent in FosB/SF and Fra-1, which is able to interact with the TATA binding protein, is required for altered cell growth.An RNA polymerase III-defective mutation in TATA-binding protein disrupts its interaction with a transcription factor IIIB subunit in drosophila cells.The TATA motif is a target for efficient transcriptional activation and nerve growth factor induction of the peripherin gene.An inverted TATA box directs downstream transcription of the bone sialoprotein gene.
P2860
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P2860
Identification of human TFIID components and direct interaction between a 250-kDa polypeptide and the TATA box-binding protein (TFIID tau).
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1992
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Identification of human TFIID ...... x-binding protein (TFIID tau).
@en
Identification of human TFIID ...... d the TATA box-binding protein
@nl
type
label
Identification of human TFIID ...... x-binding protein (TFIID tau).
@en
Identification of human TFIID ...... d the TATA box-binding protein
@nl
prefLabel
Identification of human TFIID ...... x-binding protein (TFIID tau).
@en
Identification of human TFIID ...... d the TATA box-binding protein
@nl
P2093
P2860
P356
P1476
Identification of human TFIID ...... ox-binding protein (TFIID tau)
@en
P2093
A Hoffmann
M Horikoshi
R G Roeder
S Hasegawa
Y Nakatani
P2860
P304
11809-11813
P356
10.1073/PNAS.89.24.11809
P407
P577
1992-12-01T00:00:00Z