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    GTF2F1 general transcription factor IIF subunit 1 [ Homo sapiens (human) ]

    Gene ID: 2962, updated on 3-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Leptin prevents aberrant targeting of tau to hippocampal synapses via PI 3 kinase driven inhibition of GSK3beta.

    Leptin prevents aberrant targeting of tau to hippocampal synapses via PI 3 kinase driven inhibition of GSK3β.
    Hamilton K, Morrow K, Markantoni E, Harvey J.

    11/14/2023
    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.

    Regulation of Androgen Receptor Activity by Transient Interactions of Its Transactivation Domain with General Transcription Regulators.
    De Mol E, Szulc E, Di Sanza C, Martínez-Cristóbal P, Bertoncini CW, Fenwick RB, Frigolé-Vivas M, Masín M, Hunter I, Buzón V, Brun-Heath I, García J, De Fabritiis G, Estébanez-Perpiñá E, McEwan IJ, Nebreda ÁR, Salvatella X., Free PMC Article

    12/1/2018
    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.

    Activator-mediator binding stabilizes RNA polymerase II orientation within the human mediator-RNA polymerase II-TFIIF assembly.
    Bernecky C, Taatjes DJ., Free PMC Article

    05/5/2012
    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.

    Transcriptional regulation by Pol II(G) involving mediator and competitive interactions of Gdown1 and TFIIF with Pol II.
    Jishage M, Malik S, Wagner U, Uberheide B, Ishihama Y, Hu X, Chait BT, Gnatt A, Ren B, Roeder RG., Free PMC Article

    03/31/2012
    Data show that TFIIF has an important role in stabilizing TFIIB within the PIC and after transcription initiates.

    Transcription factor TFIIF is not required for initiation by RNA polymerase II, but it is essential to stabilize transcription factor TFIIB in early elongation complexes.
    Čabart P, Újvári A, Pal M, Luse DS., Free PMC Article

    12/17/2011
    NMR and thermodynamic studies further elucidate the complex molecular mechanism by which TFIIF and FCP1 cooperate for RNAPII recycling.

    NMR structure of a complex formed by the carboxyl-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1 phosphatase.
    Yang A, Abbott KL, Desjardins A, Di Lello P, Omichinski JG, Legault P.

    01/21/2010
    Observational study of gene-disease association. (HuGE Navigator)

    Evaluating new candidate SNPs as low penetrance risk factors in sporadic breast cancer: a two-stage Spanish case-control study.
    Vega A, Salas A, Milne RL, Carracedo B, Ribas G, Ruibal A, de León AC, González-Hernández A, Benítez J, Carracedo A.

    11/5/2008
    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.

    Functional characterization of the native NH2-terminal transactivation domain of the human androgen receptor: binding kinetics for interactions with TFIIF and SRC-1a.
    Lavery DN, McEwan IJ.

    01/21/2010
    TFIIF and Rpb7 are involved in both early and late transcriptional stages

    Genomic location of the human RNA polymerase II general machinery: evidence for a role of TFIIF and Rpb7 at both early and late stages of transcription.
    Cojocaru M, Jeronimo C, Forget D, Bouchard A, Bergeron D, Côte P, Poirier GG, Greenblatt J, Coulombe B., Free PMC Article

    01/21/2010
    Interaction of TFIIF subunit RAP74 with recombinant androgen receptor N-terminal activation domain AF1 leads to imposition of helical structure on the AF1 domain.

    Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF.
    Kumar R, Betney R, Li J, Thompson EB, McEwan IJ.

    01/21/2010
    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

    Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF.
    Kamada K, Roeder RG, Burley SK., Free PMC Article

    01/21/2010
    alpha1-Helix of RAP74 is important for supporting NTP-driven translocation by RNAP II.

    Human RNA polymerase II elongation in slow motion: role of the TFIIF RAP74 alpha1 helix in nucleoside triphosphate-driven translocation.
    Zhang C, Zobeck KL, Burton ZF., Free PMC Article

    01/21/2010
    TFIIF supports elongation and suppresses pausing by stabilizing the post-translocated elongation complex

    Transcription factors IIF and IIS and nucleoside triphosphate substrates as dynamic probes of the human RNA polymerase II mechanism.
    Zhang C, Burton ZF.

    01/21/2010
    role of associated carboxyl-terminal domain phosphatase in dephosphorylating phosphoserines 2 and 5 of RNA polymerase II

    TFIIF-associating carboxyl-terminal domain phosphatase dephosphorylates phosphoserines 2 and 5 of RNA polymerase II.
    Lin PS, Dubois MF, Dahmus ME.

    01/21/2010
    NMR structure of a complex containing this TFIIF subunit and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1.

    NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1.
    Nguyen BD, Abbott KL, Potempa K, Kobor MS, Archambault J, Greenblatt J, Legault P, Omichinski JG., Free PMC Article

    01/21/2010
    The alpha 1 helix of human RAP74 has an important role in the initiation and elongation of RNA chains

    A key role for the alpha 1 helix of human RAP74 in the initiation and elongation of RNA chains.
    Funk JD, Nedialkov YA, Xu D, Burton ZF.

    01/21/2010
    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.

    Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB.
    Nguyen BD, Chen HT, Kobor MS, Greenblatt J, Legault P, Omichinski JG.

    01/21/2010
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