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TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. 再加上，我们可以发General Transcription Factor IIF, Polypeptide 1, 74kDa 抗体 (60) 和 General Transcription Factor IIF, Polypeptide 1, 74kDa 蛋白 (8)和数多这个蛋白质的别的产品。
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An AR motif of the transactivation domain has been identified that contributes to transcriptional activity by recruiting the C-terminal domain of subunit 1 of the general transcription regulator TFIIF.
These results suggest that Mediator structural shifts induced by activator binding help stably orient pol II prior to transcription initiation within the human mediator-RNA polymerase II-TFIIF assembly.
Gdown1 competes with TFIIF for binding to the RPB1 and RPB5 subunits of Pol II, thereby inhibiting an essential function of TFIIF in preinitiation complex assembly.
Data show that TFIIF has an important role in stabilizing TFIIB within the PIC and after transcription initiates.
role of associated carboxyl-terminal domain phosphatase in dephosphorylating phosphoserines 2 and 5 of RNA polymerase II
The alpha 1 helix of human RAP74 has an important role in the initiation and elongation of RNA chains
The NMR solution structure of the C-terminal domain of RAP74 has been determined, and NMR methods have been used to map the binding sites of the C-terminus of CTD phosphatase/FCP1 on the RAP74 C-terminal fragment.
cocrystal structure of the winged-helix domain of human RNA polymerase II-associating protein 74 bound to the alpha-helical C terminus of human FCP1
NMR structure of a complex containing this TFIIF subunit and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1.
Interaction of TFIIF subunit RAP74 with recombinant androgen receptor N-terminal activation domain AF1 leads to imposition of helical structure on the AF1 domain.
TFIIF supports elongation and suppresses pausing by stabilizing the post-translocated elongation complex
alpha1-Helix of RAP74 is important for supporting NTP-driven translocation by RNAP II.
TFIIF and Rpb7 are involved in both early and late transcriptional stages
Mutated hydrophobic residues in RAP74 C-terminal structure disrupt secondary structure elements, showing that binding of the androgen receptor N-terminal domain depends upon helix 3 in the winged-helix domain of the RAP74 C-terminal domain polypeptide.
NMR and thermodynamic studies further elucidate the complex molecular mechanism by which TFIIF and FCP1 cooperate for RNAPII recycling.
TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.
, general transcription factor IIF 74 kDa subunit
, general transcription factor IIF subunit 1
, transcription initiation factor IIF subunit alpha
, transcription initiation factor RAP74
, general transcription factor IIF, polypeptide 1, 74kDa
, transcription initiation factor IIF alpha subunit
, general transcription factor IIF polypeptide 1 (74kD subunit)
, RAP74 subunit of transcription factor IIF