Trans-activating domain

Trans-activating domain (TAD) is a transcription factor scaffold domain which contains binding sites for other proteins such as transcription coregulators. These binding sites are frequently referred to as activation functions (AFs).[1] TADs are named after their amino acid composition. These amino acids are either essential for the activity or simply the most abundant in the TAD. Transactivation by the Gal4 transcription factor is mediated by acidic amino acids, whereas hydrophobic residues in Gcn4 play a similar role. Hence, the TADs in Gal4 and Gcn4 are referred to as acidic or hydrophobic activation domains, respectively.[2][3][4][5][6][7][8][9] Nine-amino-acid transactivation domain (9aaTAD) defines a novel domain common to a large superfamily of eukaryotic transcription factors represented by Gal4, Oaf1, Leu3, Rtg3, Pho4, Gln3, Gcn4 in yeast and by p53, NFAT, NF-κB and VP16 in mammals.[10]

9aaTAD transcription factors p53, VP16, MLL, E2A, HSF1, NF-IL6, NFAT1 and NF-κB interact directly with the general coactivators TAF9 and CBP/p300.[11][12][13][10][14][15][16][17][18][19][20][21][22] p53 9aaTADs interact with TAF9, GCN5 and with multiple domains of CBP/p300 (KIX, TAZ1,TAZ2 and IBiD).[23][24][25][26][27]

The KIX domain of general coactivators Med15(Gal11) interacts with 9aaTAD transcription factors Gal4, Pdr1, Oaf1, Gcn4, VP16, Pho4, Msn2, Ino2 and P201.[28][29][30][31][32][33][34][35][36][37][38][39][40][41][42][43] Interactions of Gal4, Pdr1 and Gcn4 with Taf9 have been observed.[8][44][45] 9aaTAD is a common transactivation domain which recruits multiple general coactivators TAF9, MED15, CBP/p300 and GCN5.[10]

In general we can distinguish four classes of TADs:[46]

- acidic domains (called also “acid blobs” or “negative noodles", rich in D and E amino acids, present in Gal4, Gcn4 and VP16)[47]

- glutamine-rich domains (contains multiple repetitions like "QQQXXXQQQ", present in SP1)[48]

- proline-rich domains (contains repetitions like "PPPXXXPPP" present in c-jun, AP2 and Oct-2)[49]

- isoleucine-rich domains (repetitions "IIXXII", present in NTF-1)[50]

See also

References

  1. ↑ Wärnmark A, Treuter E, Wright AP, Gustafsson JA (Oct 2003). "Activation functions 1 and 2 of nuclear receptors: molecular strategies for transcriptional activation". Molecular Endocrinology 17 (10): 1901–9. doi:10.1210/me.2002-0384. PMID 12893880.
  2. ↑ Ma J, Ptashne M (Oct 1987). "A new class of yeast transcriptional activators". Cell 51 (1): 113–9. doi:10.1016/0092-8674(87)90015-8. PMID 3115591.
  3. ↑ Sadowski I, Ma J, Triezenberg S, Ptashne M (Oct 1988). "GAL4-VP16 is an unusually potent transcriptional activator". Nature 335 (6190): 563–4. Bibcode:1988Natur.335..563S. doi:10.1038/335563a0. PMID 3047590.
  4. ↑ Sullivan SM, Horn PJ, Olson VA, Koop AH, Niu W, Ebright RH, Triezenberg SJ (Oct 1998). "Mutational analysis of a transcriptional activation region of the VP16 protein of herpes simplex virus". Nucleic Acids Research 26 (19): 4487–96. doi:10.1093/nar/26.19.4487. PMC 147869. PMID 9742254.
  5. ↑ Gill G, Ptashne M (Oct 1987). "Mutants of GAL4 protein altered in an activation function". Cell 51 (1): 121–6. doi:10.1016/0092-8674(87)90016-X. PMID 3115592.
  6. ↑ Hope IA, Mahadevan S, Struhl K (Jun 1988). "Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein". Nature 333 (6174): 635–40. Bibcode:1988Natur.333..635H. doi:10.1038/333635a0. PMID 3287180.
  7. ↑ Hope IA, Struhl K (Sep 1986). "Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of yeast". Cell 46 (6): 885–94. doi:10.1016/0092-8674(86)90070-X. PMID 3530496.
  8. 1 2 Drysdale CM, Dueñas E, Jackson BM, Reusser U, Braus GH, Hinnebusch AG (Mar 1995). "The transcriptional activator GCN4 contains multiple activation domains that are critically dependent on hydrophobic amino acids". Molecular and Cellular Biology 15 (3): 1220–33. doi:10.1128/mcb.15.3.1220. PMC 230345. PMID 7862116.
  9. ↑ Regier JL, Shen F, Triezenberg SJ (Feb 1993). "Pattern of aromatic and hydrophobic amino acids critical for one of two subdomains of the VP16 transcriptional activator". Proceedings of the National Academy of Sciences of the United States of America 90 (3): 883–7. Bibcode:1993PNAS...90..883R. doi:10.1073/pnas.90.3.883. PMC 45774. PMID 8381535.
  10. 1 2 3 Piskacek S, Gregor M, Nemethova M, Grabner M, Kovarik P, Piskacek M (Jun 2007). "Nine-amino-acid transactivation domain: establishment and prediction utilities". Genomics 89 (6): 756–68. doi:10.1016/j.ygeno.2007.02.003. PMID 17467953.
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  13. ↑ Choi Y, Asada S, Uesugi M (May 2000). "Divergent hTAFII31-binding motifs hidden in activation domains". The Journal of Biological Chemistry 275 (21): 15912–6. doi:10.1074/jbc.275.21.15912. PMID 10821850.
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