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GTF2F1  -  general transcription factor IIF,...

Homo sapiens

Synonyms: BTF4, General transcription factor IIF 74 kDa subunit, General transcription factor IIF subunit 1, RAP74, TF2F1, ...
 
 
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Disease relevance of GTF2F1

  • In this work, the rates for equilibration between the active and pausing pathways were estimated in the absence of an elongation factor, in the presence of hepatitis delta antigen (HDAg), and in the presence of transcription factor IIF (TFIIF), with or without addition of SII [1].
  • A protein fraction containing transcription factors (TF) IIE and IIF was able to reconstitute transcription from the adenovirus major late promoter when added to extracts depleted of the RNA polymerase II-associating proteins RAP 30 and RAP 74 (Sopta, M., Carthew, R.W., and Greenblatt, J. (1985) J. Biol. Chem. 260, 10353-10360) [2].
  • Using these improved vectors, approximately 30 mg of soluble and active RAP74-H6 or RAP74 can be produced and purified from 1 liter of E. coli culture, representing a 10-fold improvement in protein production [3].
  • Methods were previously published for production of human RAP30 and RAP74 in bacterial cells, using a bacteriophage T7 promoter expression system [3].
 

High impact information on GTF2F1

  • The phosphorylation of RAP74 also occurs in the context of the complete TFIID complex [4].
  • However, both the N- and C-terminal kinase domains of TAFII250 are required for efficient transphosphorylation of RAP74 on serine residues [4].
  • Using a yeast interaction assay, we find that SRF binds the RAP74 subunit of TFIIF and that SRF's transcriptional activation domain is the region involved in this binding [5].
  • Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor [5].
  • A complementary DNA encoding human RAP30 has been isolated, and here we report the isolation of a cDNA encoding human RAP74 [6].
 

Biological context of GTF2F1

  • Assignment of the human GTF2F1 gene to chromosome 19p13.3 [7].
  • The role of the RAP74 alpha1 helix of transcription factor IIF (TFIIF) in stimulating elongation by human RNA polymerase II (RNAP II) was examined using millisecond-phase transient-state kinetics [8].
  • The X-ray structure of the RAP30/RAP74 interaction domains at 1.7 A resolution reveals a novel "triple barrel" dimerization fold and suggests with mutant data that interactions with the transcription apparatus are mediated not only by this tripartite beta-barrel, but also via flexible loops and alpha and beta-structures extending from it [9].
  • According to solution and mutagenesis studies, the multiple domains of RAP30 and RAP74 bind PolII, TFIIB, TAF250 and DNA in interactions that are essential for transcription initiation and elongation [9].
  • These results provide new functional and structural information on the role of phosphorylation in the recognition of acidic-rich activation domains involved in transcriptional regulation, and bring insights into how CK2 and TFIIF regulate FCP1 function [10].
 

Anatomical context of GTF2F1

  • Thus the core suppressor domain of Msx2 participates in functionally important interactions with RAP74 that regulate OC promoter activity in calvarial osteoblasts [11].
  • We have partially sequenced the RAP74 protein from purified HeLa cells, cloned its complementary DNA and shown that its translation product can interact with RAP30 in vitro as well as in vivo [12].
  • In vivo complementation of a temperature-sensitive TAFII250 cell line reveals that the RAP74 interaction is critical for cell viability [13].
  • Our data are consistent with the possibility that in living Chironomus salivary gland cells, DRB interferes with the recruitment of TFIIF, but not of TFIIH, to the promoter by interference with the activity of the CK2alpha subunit enzyme and phosphorylation of RAP74 and thereby DRB blocks transcription initiation [14].
 

Associations of GTF2F1 with chemical compounds

  • During elongation, TFIIF 74(1-158) fails to support detectable nucleoside triphosphate (NTP)-driven translocation from a stall position and is notably defective in supporting bond completion (NTP-driven translocation coupled to pyrophosphate release) during the processive transition between bonds [8].
  • Human RNA polymerase II elongation in slow motion: role of the TFIIF RAP74 alpha1 helix in nucleoside triphosphate-driven translocation [8].
  • The CK2 site adjacent to the RAP74-binding site in the carboxyl-terminal domain can be phosphorylated at three successive serine residues (S942-S944), with phosphorylations at S942 and S944 both contributing to enhanced binding to RAP74 [10].
  • The CK2 site adjacent to the RAP74-binding site in the central domain of FCP1 is phosphorylated at a single threonine site (T584) [10].
  • High-resolution PAGE confirmed that the radioactive species associated with RAP30 and RAP74 were ADP-ribose polymers [15].
 

Physical interactions of GTF2F1

  • RAP74 binds to the N-terminal region of RAP30 between amino acids 1 and 98 [16].
  • Our results demonstrate that the recombinant AR AF1 can acquire significantly higher helical content after interacting with RAP74, a subunit of the TFIIF complex [17].
  • The C-terminal region of RAP74 (amino acids 358-517) binds directly and independently to TFIIB [16].
  • Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation [13].
  • RAP74 had an activity of enhancing the binding of the bacterial RNA polymerase to the promoter [18].
 

Enzymatic interactions of GTF2F1

  • Further analyses using deletion mutants of RAP74 revealed that amino acid residues 206-256 are phosphorylated by the TFIID fraction [19].
 

Regulatory relationships of GTF2F1

  • In addition, TFIIE and RAP74 strongly stimulated cross-linking of RAP30 and the large subunits of RNA polymerase II to position -19 [20].
 

Other interactions of GTF2F1

  • Mutants were tested for accurate transcriptional activity, RAP74 binding, and TFIIB binding [16].
  • In a protein interaction assay, c-myc1-143 bound selectively to two basal transcription factors, the TATA binding protein (TBP) and the RAP74 subunit of TFIIF [21].
  • A cDNA encoding RAP74, a general initiation factor for transcription by RNA polymerase II [6].
  • RAP74 deletion mutants RAP74(1-227), which includes an intact alpha1 helix, and RAP74(1-158), in which the alpha1 helix is deleted, were compared [8].
  • Enhanced binding of RNAP II CTD phosphatase FCP1 to RAP74 following CK2 phosphorylation [10].
 

Analytical, diagnostic and therapeutic context of GTF2F1

References

  1. Combinatorial control of human RNA polymerase II (RNAP II) pausing and transcript cleavage by transcription factor IIF, hepatitis delta antigen, and stimulatory factor II. Zhang, C., Yan, H., Burton, Z.F. J. Biol. Chem. (2003) [Pubmed]
  2. Factors involved in specific transcription by mammalian RNA polymerase II. RNA polymerase II-associating protein 30 is an essential component of transcription factor IIF. Flores, O., Maldonado, E., Burton, Z., Greenblatt, J., Reinberg, D. J. Biol. Chem. (1988) [Pubmed]
  3. Importance of codon preference for production of human RAP74 and reconstitution of the RAP30/74 complex. Wang, B.Q., Lei, L., Burton, Z.F. Protein Expr. Purif. (1994) [Pubmed]
  4. TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74. Dikstein, R., Ruppert, S., Tjian, R. Cell (1996) [Pubmed]
  5. Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor. Joliot, V., Demma, M., Prywes, R. Nature (1995) [Pubmed]
  6. A cDNA encoding RAP74, a general initiation factor for transcription by RNA polymerase II. Finkelstein, A., Kostrub, C.F., Li, J., Chavez, D.P., Wang, B.Q., Fang, S.M., Greenblatt, J., Burton, Z.F. Nature (1992) [Pubmed]
  7. Assignment of the human GTF2F1 gene to chromosome 19p13.3. Aso, T., Tsai, P., Kawaguchi, T., Menninger, J.C., Kitajima, S., Yasukochi, Y., Ward, D.C., Weissman, S.M. Genomics (1993) [Pubmed]
  8. Human RNA polymerase II elongation in slow motion: role of the TFIIF RAP74 alpha1 helix in nucleoside triphosphate-driven translocation. Zhang, C., Zobeck, K.L., Burton, Z.F. Mol. Cell. Biol. (2005) [Pubmed]
  9. Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution. Gaiser, F., Tan, S., Richmond, T.J. J. Mol. Biol. (2000) [Pubmed]
  10. Enhanced binding of RNAP II CTD phosphatase FCP1 to RAP74 following CK2 phosphorylation. Abbott, K.L., Renfrow, M.B., Chalmers, M.J., Nguyen, B.D., Marshall, A.G., Legault, P., Omichinski, J.G. Biochemistry (2005) [Pubmed]
  11. Structure-function analysis of Msx2-mediated transcriptional suppression. Newberry, E.P., Latifi, T., Battaile, J.T., Towler, D.A. Biochemistry (1997) [Pubmed]
  12. Characterization of cDNA for the large subunit of the transcription initiation factor TFIIF. Aso, T., Vasavada, H.A., Kawaguchi, T., Germino, F.J., Ganguly, S., Kitajima, S., Weissman, S.M., Yasukochi, Y. Nature (1992) [Pubmed]
  13. Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation. Ruppert, S., Tjian, R. Genes Dev. (1995) [Pubmed]
  14. The binding of the alpha subunit of protein kinase CK2 and RAP74 subunit of TFIIF to protein-coding genes in living cells is DRB sensitive. Egyházi, E., Ossoinak, A., Filhol-Cochet, O., Cochet, C., Pigon, A. Mol. Cell. Biochem. (1999) [Pubmed]
  15. TFIIF, a basal eukaryotic transcription factor, is a substrate for poly(ADP-ribosyl)ation. Rawling, J.M., Alvarez-Gonzalez, R. Biochem. J. (1997) [Pubmed]
  16. RNA polymerase II-associated protein (RAP) 74 binds transcription factor (TF) IIB and blocks TFIIB-RAP30 binding. Fang, S.M., Burton, Z.F. J. Biol. Chem. (1996) [Pubmed]
  17. Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF. Kumar, R., Betney, R., Li, J., Thompson, E.B., McEwan, I.J. Biochemistry (2004) [Pubmed]
  18. Enhancement of bacterial transcription initiation in vitro by the 74 kDa subunit of human general transcription factor IIF (RAP74). Chibazakura, T., Kitajima, S., Yonaha, M., Yasukochi, Y. Biochim. Biophys. Acta (1994) [Pubmed]
  19. Cell-cycle-dependent phosphorylation of the basal transcription factor RAP74. Yonaha, M., Tsuchiya, T., Yasukochi, Y. FEBS Lett. (1997) [Pubmed]
  20. Localization of subunits of transcription factors IIE and IIF immediately upstream of the transcriptional initiation site of the adenovirus major late promoter. Robert, F., Forget, D., Li, J., Greenblatt, J., Coulombe, B. J. Biol. Chem. (1996) [Pubmed]
  21. Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding. McEwan, I.J., Dahlman-Wright, K., Ford, J., Wright, A.P. Biochemistry (1996) [Pubmed]
  22. RAP30/74: a general initiation factor that binds to RNA polymerase II. Burton, Z.F., Killeen, M., Sopta, M., Ortolan, L.G., Greenblatt, J. Mol. Cell. Biol. (1988) [Pubmed]
  23. RNA polymerase II/TFIIF structure and conserved organization of the initiation complex. Chung, W.H., Craighead, J.L., Chang, W.H., Ezeokonkwo, C., Bareket-Samish, A., Kornberg, R.D., Asturias, F.J. Mol. Cell (2003) [Pubmed]
  24. Factors involved in specific transcription by mammalian RNA polymerase II. Purification and subunit composition of transcription factor IIF. Flores, O., Ha, I., Reinberg, D. J. Biol. Chem. (1990) [Pubmed]
 
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