The TATA-box-binding protein (TBP) is a crucial component of the transcription machinery in archaea and eukaryotic organisms [1]. It acts as a central transcription factor that associates with the core promoter and serves as a nexus for gene regulation through its interactions with other factors [2]. TBP is essential for the initiation of transcription by all three nuclear RNA polymerases and is required for the assembly of transcription preinitiation complexes on genes transcribed by these polymerases [3][4][5][6][7][8][9][10][11][12]. Additionally, TBP plays a role in the regulation of cellular proliferation and is a frequent target for transcriptional regulators [13]. It is also involved in the stress-mediated G2 checkpoint and negatively regulates cell cycle progression [14]. TBP contains a concave surface that interacts specifically with TATA promoter elements and a convex surface that mediates protein-protein interactions with general and gene-specific transcription factors [15]. Furthermore, TBP is an essential transcription initiation factor in both Archaea and Eucarya [9]. The protein is also subject to regulation by various cellular signaling pathways, such as Ras cellular signaling and c-Jun N-Terminal Kinase 1 and 2 [6]. TBP is a universal transcription factor that nucleates the assembly of transcription preinitiation complexes on genes transcribed by all three RNA polymerases [10]. It is also involved in interactions with other proteins, such as general transcription factor TFIIA and transcriptional repressor NC2 [16]. Moreover, TBP is a target for regulation by specific E3 ligase/deubiquitinase pairs during muscle differentiation [17]. These findings collectively highlight the central and multifaceted role of TBP in transcriptional regulation and cellular processes.
References:
[1] Á. Santiago, R. Razo‐Hernández, & N. Pastor, "Revealing the structural contributions to thermal adaptation of the tata-box binding protein: molecular dynamics and qspr analyses", Journal of Chemical Information and Modeling, vol. 60, no. 2, p. 866-879, 2020. https://doi.org/10.1021/acs.jcim.9b00824
[2] F. Xiu, H. Shi, K. Adelman, & J. Lis, "Probing tbp interactions in transcription initiation and reinitiation with rna aptamers that act in distinct modes", Proceedings of the National Academy of Sciences, vol. 101, no. 18, p. 6934-6939, 2004. https://doi.org/10.1073/pnas.0401523101
[3] R. Ganster, W. Shen, & M. Schmidt, "Isolation of std1, a high-copy-number suppressor of a dominant negative mutation in the yeast tata-binding protein.", Molecular and Cellular Biology, vol. 13, no. 6, p. 3650-3659, 1993. https://doi.org/10.1128/mcb.13.6.3650
[4] J. Wu, K. Parkhurst, R. Powell, M. Brenowitz, & L. Parkhurst, "Dna bends in tata-binding protein·tata complexes in solution are dna sequence-dependent", Journal of Biological Chemistry, vol. 276, no. 18, p. 14614-14622, 2001. https://doi.org/10.1074/jbc.m004402200
[5] J. Prigge and E. Schmidt, "Interaction of protein inhibitor of activated stat (pias) proteins with the tata-binding protein, tbp", Journal of Biological Chemistry, vol. 281, no. 18, p. 12260-12269, 2006. https://doi.org/10.1074/jbc.m510835200
[6] S. Johnson, N. Mandavia, H. Wang, & D. Johnson, "Transcriptional regulation of the tata-binding protein by ras cellular signaling", Molecular and Cellular Biology, vol. 20, no. 14, p. 5000-5009, 2000. https://doi.org/10.1128/mcb.20.14.5000-5009.2000
[7] J. Steffan, D. Keys, J. Dodd, & M. Nomura, "The role of tbp in rdna transcription by rna polymerase i in saccharomyces cerevisiae: tbp is required for upstream activation factor-dependent recruitment of core factor.", Genes & Development, vol. 10, no. 20, p. 2551-2563, 1996. https://doi.org/10.1101/gad.10.20.2551
[8] S. Zhong, J. Fromm, & D. Johnson, "Tbp is differentially regulated by c-jun n-terminal kinase 1 (jnk1) and jnk2 through elk-1, controlling c-jun expression and cell proliferation", Molecular and Cellular Biology, vol. 27, no. 1, p. 54-64, 2007. https://doi.org/10.1128/mcb.01365-06
[9] B. Brindefalk, B. Dessailly, C. Yeats, C. Orengo, F. Werner, & A. Poole, "Evolutionary history of the tbp-domain superfamily", Nucleic Acids Research, vol. 41, no. 5, p. 2832-2845, 2013. https://doi.org/10.1093/nar/gkt045
[10] E. Maldonado, "Transcriptional functions of a new mammalian tata-binding protein-related factor", Journal of Biological Chemistry, vol. 274, no. 19, p. 12963-12966, 1999. https://doi.org/10.1074/jbc.274.19.12963
[11] D. Auble, "The dynamic personality of tata-binding protein", Trends in Biochemical Sciences, vol. 34, no. 2, p. 49-52, 2009. https://doi.org/10.1016/j.tibs.2008.10.008
[12] S. Johnson, L. Dubeau, M. Kawalek, A. Dervan, A. Schönthal, C. Danget al., "Increased expression of tata-binding protein, the central transcription factor, can contribute to oncogenesis", Molecular and Cellular Biology, vol. 23, no. 9, p. 3043-3051, 2003. https://doi.org/10.1128/mcb.23.9.3043-3051.2003
[13] G. Zheng and Y. Yi, "Znf76, a novel transcriptional repressor targeting tata-binding protein, is modulated by sumoylation", Journal of Biological Chemistry, vol. 279, no. 41, p. 42410-42421, 2004. https://doi.org/10.1074/jbc.m407287200
[14] M. Shimada, T. Nakadai, & T. Tamura, "Tata-binding protein-like protein (tlp/trf2/tlf) negatively regulates cell cycle progression and is required for the stress-mediated g2 checkpoint", Molecular and Cellular Biology, vol. 23, no. 12, p. 4107-4120, 2003. https://doi.org/10.1128/mcb.23.12.4107-4120.2003
[15] M. Lee and K. Struhl, "Mutations on the dna-binding surface of tata-binding protein can specifically impair the response to acidic activators in vivo", Molecular and Cellular Biology, vol. 15, no. 10, p. 5461-5469, 1995. https://doi.org/10.1128/mcb.15.10.5461
[16] Y. Kim, Y. Ebright, A. Goodman, D. Reinberg, & R. Ebright, "Nonradioactive, ultrasensitive site-specific protein–protein photocrosslinking: interactions of α-helix 2 of tata-binding protein with general transcription factor tfiia and transcriptional repressor nc2", Nucleic Acids Research, vol. 36, no. 19, p. 6143-6154, 2008. https://doi.org/10.1093/nar/gkn612
[17] L. Li, S. Martinez, W. Hu, Z. Liu, & R. Tjian, "A specific e3 ligase/deubiquitinase pair modulates tbp protein levels during muscle differentiation", Elife, vol. 4, 2015. https://doi.org/10.7554/elife.08536
