Alternative titles; symbols
HGNC Approved Gene Symbol: TAF5
Cytogenetic location: 10q24.33 Genomic coordinates (GRCh38): 10:103,367,976-103,389,065 (from NCBI)
The multisubunit TFIID is the DNA-binding component of the transcriptional machinery of RNA polymerase II (see POLR2A; 180660). TFIID is composed of TATA box-binding protein (TBP; 600075) and TBP-associated factors, or TAFs (see 313650).
Dubrovskaya et al. (1996) characterized a human TAF, called TAFII100 by them, which is homologous to Drosophila TAFII80 (65% similar) and yeast TAFII90 (57% similar). They cloned a TAFII100 cDNA that encodes a 799-amino acid polypeptide with a calculated molecular mass of 87.9 kD; however, both endogenous and recombinant proteins have an electrophoretically determined relative mass of 100 kD. By deletional analysis, Dubrovskaya et al. (1996) showed that the C-terminal, WD-40 repeat-containing domain is not required for incorporation into the TFIID complex.
Independently, Tanese et al. (1996) cloned and characterized the C-terminal 801 amino acids of TAFII100. They suggested that, since the N-terminal amino acid sequence obtained from sequencing the endogenous protein is different from the N-terminal sequence predicted by the cloned gene, the full-length TAFII100 gene (also symbolized TAF2D) probably encodes a short peptide sequence upstream of their putative initiation methionine and that of Dubrovskaya et al. (1996).
Dubrovskaya et al. (1996) demonstrated that specific interaction between TFIIF/RAP30 (189969) and TAFII100 supports in vitro polII preinitiation complex formation in the presence of TFIID.
Tao et al. (1997) used immunoprecipitation studies to show that human TAFII100 is an integral subunit associated with all transcriptionally competent forms of TF2D. They also showed that anti-TAFII100 antibodies selectively inhibited basal transcription from a TATA-less promoter relative to a TATA-containing promoter.
Cryoelectron Microscopy
Bieniossek et al. (2013) presented the structure of the human core-TFIID complex, consisting of 2 copies each of TAF4 (601796), TAF5, TAF6 (602955), TAF9 (600822), and TAF12 (600773), determined by cryoelectron microscopy at 11.6-angstrom resolution. The structure revealed a 2-fold symmetric, interlaced architecture, with pronounced protrusions, that accommodates all conserved structural features of the TAFs including the histone folds. Bieniossek et al. (2013) further demonstrated that binding of 1 TAF8 (609514)-TAF10 (600475) complex breaks the original symmetry of the core-TFIID. Bieniossek et al. (2013) proposed that the resulting asymmetric structure serves as a functional scaffold to nucleate holo-TFIID assembly, by accreting 1 copy each of the remaining TAFs and TBP.
Dubrovskaya et al. (1996) mapped the TAF5 (TAF2D) gene to chromosome 10q24-q25.2 by Southern analysis of human-hamster hybrid cell line genomic DNA and by in situ hybridization.
Bieniossek, C., Papai, G., Schaffitzel, C., Garzoni, F., Chaillet, M., Scheer, E., Papadopoulos, P., Tora, L., Schultz, P., Berger, I. The architecture of human general transcription factor TFIID core complex. Nature 493: 699-702, 2013. [PubMed: 23292512] [Full Text: https://doi.org/10.1038/nature11791]
Dubrovskaya, V., Lavigne, A.-C., Davidson, I., Acker, J., Staub, A., Tora, L. Distinct domains of hTAFII100 are required for functional interaction with transcription factor TFIIF-beta (RAP30) and incorporation into the TFIID complex. EMBO J. 15: 3702-3712, 1996. [PubMed: 8758937]
Dubrovskaya, V., Mattei, M.-G., Tora, L. Localization of the gene (TAF2D) encoding the 100-kDa subunit (hTAFII100) of the human TFIID complex to chromosome 10 band q24-q25.2. Genomics 36: 556-557, 1996. [PubMed: 8884287] [Full Text: https://doi.org/10.1006/geno.1996.0509]
Tanese, N., Saluja, D., Vassallo, M. F., Chen, J.-L., Admon, A. Molecular cloning and analysis of two subunits of the human TFIID complex: hTAFII130 and hTAFII100. Proc. Nat. Acad. Sci. 93: 13611-13616, 1996. [PubMed: 8942982] [Full Text: https://doi.org/10.1073/pnas.93.24.13611]
Tao, Y., Guermah, M., Martinez, E., Oelgeschlager, T., Hasegawa, S., Takada, R., Yamamoto, T., Horikoshi, M., Roeder, R. G. Specific interactions and potential functions of human TAF(II)100. J. Biol. Chem. 272: 6714-6721, 1997. [PubMed: 9045704] [Full Text: https://doi.org/10.1074/jbc.272.10.6714]