Alternative titles; symbols
HGNC Approved Gene Symbol: GTF2F2
Cytogenetic location: 13q14.12-q14.13 Genomic coordinates (GRCh38) : 13:45,120,510-45,284,893 (from NCBI)
The RNA polymerase II transcription factor TFIIF is a heterodimer with 2 subunits: one, referred to as RAP74, of approximately 70 kD (189968) and the other, known as RAP30 or GTF2F2, of 30 kD. TFIIF affects RNA polymerase II activity both during the initiation and elongation stages of RNA transcription (summary by Tan et al., 1995).
Sopta et al. (1989) purified RAP30 from HeLa cells and raised an antibody to the protein, which was then used to screen an expression cDNA library from the promyelocytic leukemia cell line, HL60. The predicted protein was 234 amino acids in length. Subsequently, Horikoshi et al. (1991) corrected the RAP30 cDNA sequence to show that the predicted protein is actually 249 amino acids. TFIIF appears to assist TFIIB (189963) in recruiting RNA polymerase II into a preinitiation complex. It also affects RNA transcription by suppressing transient pausing of the polymerase at locations on the DNA template. Tan et al. (1995) showed that these 2 activities are controlled by distinct functional domains. The initiation activity is mediated by RAP30 C-terminal sequences (which include a DNA binding domain) and the elongation activity is mediated by sequences immediately upstream of the C terminus, where RNA polymerase II is thought to bind, as well as by sequences near the RAP30 N terminus.
Horikoshi, M., Fujita, H., Wang, J., Takada, R., Roeder, R. G. Nucleotide and amino acid sequence of RAP30. Nucleic Acids Res. 19: 5436 only, 1991. [PubMed: 1840667] [Full Text: https://doi.org/10.1093/nar/19.19.5436]
Sopta, M., Burton, Z. F., Greenblatt, J. Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II. Nature 341: 410-414, 1989. [PubMed: 2477704] [Full Text: https://doi.org/10.1038/341410a0]
Tan, S., Conaway, R. C., Conaway, J. W. Dissection of transcription factor TFIIF functional domains required for initiation and elongation. Proc. Nat. Acad. Sci. 92: 6042-6046, 1995. [PubMed: 7597077] [Full Text: https://doi.org/10.1073/pnas.92.13.6042]