Skip to main content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
EMBO J. 1994 Jul 1; 13(13): 3039–3049.
doi: 10.1002/j.1460-2075.1994.tb06603.x
PMCID: PMC395194
PMID: 8039499

Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor.

D Barettino, M M Vivanco Ruiz, and H G Stunnenberg
Author information Copyright and License information PMC Disclaimer

Abstract

Transcriptional activation by nuclear receptors is achieved through autonomous activation functions (AFs), a constitutive N-terminal AF-1 and a C-terminal, ligand-dependent AF-2 that comprises a motif conserved between nuclear receptors. We have performed an extensive mutational analysis of the putative AF-2 domain of chicken thyroid hormone receptor alpha (cT3R alpha). We show that the AF-2 region mediates transactivation as well as transcriptional interference (squelching), not only between the thyroid hormone and vitamin (type II) receptors, but also between type II and steroid hormone (type I) receptors. Transcriptional activation and interference require equivalent doses of the cognate ligand, and mutations in the conserved motif that reduce ligand-induced transactivation also impair transcriptional interference. When fused to the Gal4 DNA binding domain, a 35 amino acid long fragment containing the conserved motif is able to transactivate and squelch, albeit in a ligand-independent manner. Our results define the AF-2 of cT3R alpha as an autonomous transactivation domain that, in its natural context, is governed by ligand. We propose that AF-2 is probably part of a surface for interaction with either a general transcription factor or a putative bridging factor, that might be utilized by type I and II receptors.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (2.3M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

 
icon of scanned page 3039
3039
icon of scanned page 3040
3040
icon of scanned page 3041
3041
icon of scanned page 3042
3042
icon of scanned page 3043
3043
icon of scanned page 3044
3044
icon of scanned page 3045
3045
icon of scanned page 3046
3046
icon of scanned page 3047
3047
icon of scanned page 3048
3048
icon of scanned page 3049
3049
 

Images in this article

Image

Image
on p.3045

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  • Allan GF, Leng X, Tsai SY, Weigel NL, Edwards DP, Tsai MJ, O'Malley BW. Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation. J Biol Chem. 1992 Sep 25;267(27):19513–19520. [PubMed] [Google Scholar]
  • Allan GF, Tsai SY, Tsai MJ, O'Malley BW. Ligand-dependent conformational changes in the progesterone receptor are necessary for events that follow DNA binding. Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11750–11754. [PMC free article] [PubMed] [Google Scholar]
  • Arriza JL, Weinberger C, Cerelli G, Glaser TM, Handelin BL, Housman DE, Evans RM. Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor. Science. 1987 Jul 17;237(4812):268–275. [PubMed] [Google Scholar]
  • Baes M, Gulick T, Choi HS, Martinoli MG, Simha D, Moore DD. A new orphan member of the nuclear hormone receptor superfamily that interacts with a subset of retinoic acid response elements. Mol Cell Biol. 1994 Mar;14(3):1544–1552. [PMC free article] [PubMed] [Google Scholar]
  • Baker AR, McDonnell DP, Hughes M, Crisp TM, Mangelsdorf DJ, Haussler MR, Pike JW, Shine J, O'Malley BW. Cloning and expression of full-length cDNA encoding human vitamin D receptor. Proc Natl Acad Sci U S A. 1988 May;85(10):3294–3298. [PMC free article] [PubMed] [Google Scholar]
  • Baniahmad A, Steiner C, Köhne AC, Renkawitz R. Modular structure of a chicken lysozyme silencer: involvement of an unusual thyroid hormone receptor binding site. Cell. 1990 May 4;61(3):505–514. [PubMed] [Google Scholar]
  • Baniahmad A, Köhne AC, Renkawitz R. A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor. EMBO J. 1992 Mar;11(3):1015–1023. [PMC free article] [PubMed] [Google Scholar]
  • Baniahmad A, Ha I, Reinberg D, Tsai S, Tsai MJ, O'Malley BW. Interaction of human thyroid hormone receptor beta with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone. Proc Natl Acad Sci U S A. 1993 Oct 1;90(19):8832–8836. [PMC free article] [PubMed] [Google Scholar]
  • Barettino D, Bugge TH, Bartunek P, Vivanco Ruiz MD, Sonntag-Buck V, Beug H, Zenke M, Stunnenberg HG. Unliganded T3R, but not its oncogenic variant, v-erbA, suppresses RAR-dependent transactivation by titrating out RXR. EMBO J. 1993 Apr;12(4):1343–1354. [PMC free article] [PubMed] [Google Scholar]
  • Barettino D, Feigenbutz M, Valcárcel R, Stunnenberg HG. Improved method for PCR-mediated site-directed mutagenesis. Nucleic Acids Res. 1994 Feb 11;22(3):541–542. [PMC free article] [PubMed] [Google Scholar]
  • Becker-André M, André E, DeLamarter JF. Identification of nuclear receptor mRNAs by RT-PCR amplification of conserved zinc-finger motif sequences. Biochem Biophys Res Commun. 1993 Aug 16;194(3):1371–1379. [PubMed] [Google Scholar]
  • Beekman JM, Allan GF, Tsai SY, Tsai MJ, O'Malley BW. Transcriptional activation by the estrogen receptor requires a conformational change in the ligand binding domain. Mol Endocrinol. 1993 Oct;7(10):1266–1274. [PubMed] [Google Scholar]
  • Berkenstam A, Vivanco Ruiz MM, Barettino D, Horikoshi M, Stunnenberg HG. Cooperativity in transactivation between retinoic acid receptor and TFIID requires an activity analogous to E1A. Cell. 1992 May 1;69(3):401–412. [PubMed] [Google Scholar]
  • Bhat MK, Parkison C, McPhie P, Liang CM, Cheng SY. Conformational changes of human beta 1 thyroid hormone receptor induced by binding of 3,3',5-triiodo-L-thyronine. Biochem Biophys Res Commun. 1993 Aug 31;195(1):385–392. [PubMed] [Google Scholar]
  • Bocquel MT, Kumar V, Stricker C, Chambon P, Gronemeyer H. The contribution of the N- and C-terminal regions of steroid receptors to activation of transcription is both receptor and cell-specific. Nucleic Acids Res. 1989 Apr 11;17(7):2581–2595. [PMC free article] [PubMed] [Google Scholar]
  • Bodine PV, Schmidt TJ, Litwack G. Evidence that pH induced activation of the rat hepatic glucocorticoid-receptor complex is irreversible. J Steroid Biochem. 1984 Mar;20(3):683–689. [PubMed] [Google Scholar]
  • Chang C, Kokontis J. Identification of a new member of the steroid receptor super-family by cloning and sequence analysis. Biochem Biophys Res Commun. 1988 Sep 15;155(2):971–977. [PubMed] [Google Scholar]
  • Choy B, Green MR. Eukaryotic activators function during multiple steps of preinitiation complex assembly. Nature. 1993 Dec 9;366(6455):531–536. [PubMed] [Google Scholar]
  • Danielian PS, White R, Lees JA, Parker MG. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J. 1992 Mar;11(3):1025–1033. [PMC free article] [PubMed] [Google Scholar]
  • Davis IJ, Hazel TG, Chen RH, Blenis J, Lau LF. Functional domains and phosphorylation of the orphan receptor Nur77. Mol Endocrinol. 1993 Aug;7(8):953–964. [PubMed] [Google Scholar]
  • de Thé H, Marchio A, Tiollais P, Dejean A. A novel steroid thyroid hormone receptor-related gene inappropriately expressed in human hepatocellular carcinoma. Nature. 1987 Dec 17;330(6149):667–670. [PubMed] [Google Scholar]
  • Dreyer C, Krey G, Keller H, Givel F, Helftenbein G, Wahli W. Control of the peroxisomal beta-oxidation pathway by a novel family of nuclear hormone receptors. Cell. 1992 Mar 6;68(5):879–887. [PubMed] [Google Scholar]
  • Folkers GE, van der Leede BJ, van der Saag PT. The retinoic acid receptor-beta 2 contains two separate cell-specific transactivation domains, at the N-terminus and in the ligand-binding domain. Mol Endocrinol. 1993 Apr;7(4):616–627. [PubMed] [Google Scholar]
  • Fondell JD, Roy AL, Roeder RG. Unliganded thyroid hormone receptor inhibits formation of a functional preinitiation complex: implications for active repression. Genes Dev. 1993 Jul;7(7B):1400–1410. [PubMed] [Google Scholar]
  • Forman BM, Samuels HH. Interactions among a subfamily of nuclear hormone receptors: the regulatory zipper model. Mol Endocrinol. 1990 Sep;4(9):1293–1301. [PubMed] [Google Scholar]
  • Fritsch M, Leary CM, Furlow JD, Ahrens H, Schuh TJ, Mueller GC, Gorski J. A ligand-induced conformational change in the estrogen receptor is localized in the steroid binding domain. Biochemistry. 1992 Jun 16;31(23):5303–5311. [PubMed] [Google Scholar]
  • Giguere V, Ong ES, Segui P, Evans RM. Identification of a receptor for the morphogen retinoic acid. Nature. 1987 Dec 17;330(6149):624–629. [PubMed] [Google Scholar]
  • Giguère V, Yang N, Segui P, Evans RM. Identification of a new class of steroid hormone receptors. Nature. 1988 Jan 7;331(6151):91–94. [PubMed] [Google Scholar]
  • Goodrich JA, Hoey T, Thut CJ, Admon A, Tjian R. Drosophila TAFII40 interacts with both a VP16 activation domain and the basal transcription factor TFIIB. Cell. 1993 Nov 5;75(3):519–530. [PubMed] [Google Scholar]
  • Green S, Walter P, Kumar V, Krust A, Bornert JM, Argos P, Chambon P. Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature. 1986 Mar 13;320(6058):134–139. [PubMed] [Google Scholar]
  • Green S, Issemann I, Sheer E. A versatile in vivo and in vitro eukaryotic expression vector for protein engineering. Nucleic Acids Res. 1988 Jan 11;16(1):369–369. [PMC free article] [PubMed] [Google Scholar]
  • Gronemeyer H. Control of transcription activation by steroid hormone receptors. FASEB J. 1992 May;6(8):2524–2529. [PubMed] [Google Scholar]
  • Ha I, Lane WS, Reinberg D. Cloning of a human gene encoding the general transcription initiation factor IIB. Nature. 1991 Aug 22;352(6337):689–695. [PubMed] [Google Scholar]
  • Hazel TG, Nathans D, Lau LF. A gene inducible by serum growth factors encodes a member of the steroid and thyroid hormone receptor superfamily. Proc Natl Acad Sci U S A. 1988 Nov;85(22):8444–8448. [PMC free article] [PubMed] [Google Scholar]
  • Hoey T, Weinzierl RO, Gill G, Chen JL, Dynlacht BD, Tjian R. Molecular cloning and functional analysis of Drosophila TAF110 reveal properties expected of coactivators. Cell. 1993 Jan 29;72(2):247–260. [PubMed] [Google Scholar]
  • Hollenberg SM, Evans RM. Multiple and cooperative trans-activation domains of the human glucocorticoid receptor. Cell. 1988 Dec 2;55(5):899–906. [PubMed] [Google Scholar]
  • Honda S, Morohashi K, Nomura M, Takeya H, Kitajima M, Omura T. Ad4BP regulating steroidogenic P-450 gene is a member of steroid hormone receptor superfamily. J Biol Chem. 1993 Apr 5;268(10):7494–7502. [PubMed] [Google Scholar]
  • Ikeda Y, Lala DS, Luo X, Kim E, Moisan MP, Parker KL. Characterization of the mouse FTZ-F1 gene, which encodes a key regulator of steroid hydroxylase gene expression. Mol Endocrinol. 1993 Jul;7(7):852–860. [PubMed] [Google Scholar]
  • Ing NH, Beekman JM, Tsai SY, Tsai MJ, O'Malley BW. Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II). J Biol Chem. 1992 Sep 5;267(25):17617–17623. [PubMed] [Google Scholar]
  • Ingles CJ, Shales M, Cress WD, Triezenberg SJ, Greenblatt J. Reduced binding of TFIID to transcriptionally compromised mutants of VP16. Nature. 1991 Jun 13;351(6327):588–590. [PubMed] [Google Scholar]
  • Jantzen HM, Strähle U, Gloss B, Stewart F, Schmid W, Boshart M, Miksicek R, Schütz G. Cooperativity of glucocorticoid response elements located far upstream of the tyrosine aminotransferase gene. Cell. 1987 Apr 10;49(1):29–38. [PubMed] [Google Scholar]
  • Kastner P, Krust A, Turcotte B, Stropp U, Tora L, Gronemeyer H, Chambon P. Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B. EMBO J. 1990 May;9(5):1603–1614. [PMC free article] [PubMed] [Google Scholar]
  • Keaveney M, Berkenstam A, Feigenbutz M, Vriend G, Stunnenberg HG. Residues in the TATA-binding protein required to mediate a transcriptional response to retinoic acid in EC cells. Nature. 1993 Oct 7;365(6446):562–566. [PubMed] [Google Scholar]
  • Keidel S, LeMotte P, Apfel C. Different agonist- and antagonist-induced conformational changes in retinoic acid receptors analyzed by protease mapping. Mol Cell Biol. 1994 Jan;14(1):287–298. [PMC free article] [PubMed] [Google Scholar]
  • Koelle MR, Talbot WS, Segraves WA, Bender MT, Cherbas P, Hogness DS. The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily. Cell. 1991 Oct 4;67(1):59–77. [PubMed] [Google Scholar]
  • Krust A, Kastner P, Petkovich M, Zelent A, Chambon P. A third human retinoic acid receptor, hRAR-gamma. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5310–5314. [PMC free article] [PubMed] [Google Scholar]
  • Ladias JA, Karathanasis SK. Regulation of the apolipoprotein AI gene by ARP-1, a novel member of the steroid receptor superfamily. Science. 1991 Feb 1;251(4993):561–565. [PubMed] [Google Scholar]
  • Landt O, Grunert HP, Hahn U. A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene. 1990 Nov 30;96(1):125–128. [PubMed] [Google Scholar]
  • Lavorgna G, Ueda H, Clos J, Wu C. FTZ-F1, a steroid hormone receptor-like protein implicated in the activation of fushi tarazu. Science. 1991 May 10;252(5007):848–851. [PubMed] [Google Scholar]
  • Lazar MA, Hodin RA, Darling DS, Chin WW. A novel member of the thyroid/steroid hormone receptor family is encoded by the opposite strand of the rat c-erbA alpha transcriptional unit. Mol Cell Biol. 1989 Mar;9(3):1128–1136. [PMC free article] [PubMed] [Google Scholar]
  • Lazar MA, Jones KE, Chin WW. Isolation of a cDNA encoding human Rev-ErbA alpha: transcription from the noncoding DNA strand of a thyroid hormone receptor gene results in a related protein that does not bind thyroid hormone. DNA Cell Biol. 1990 Mar;9(2):77–83. [PubMed] [Google Scholar]
  • Lee WS, Kao CC, Bryant GO, Liu X, Berk AJ. Adenovirus E1A activation domain binds the basic repeat in the TATA box transcription factor. Cell. 1991 Oct 18;67(2):365–376. [PubMed] [Google Scholar]
  • Leid M, Kastner P, Chambon P. Multiplicity generates diversity in the retinoic acid signalling pathways. Trends Biochem Sci. 1992 Oct;17(10):427–433. [PubMed] [Google Scholar]
  • Lewin B. Commitment and activation at pol II promoters: a tail of protein-protein interactions. Cell. 1990 Jun 29;61(7):1161–1164. [PubMed] [Google Scholar]
  • Lin YS, Green MR. Mechanism of action of an acidic transcriptional activator in vitro. Cell. 1991 Mar 8;64(5):971–981. [PubMed] [Google Scholar]
  • Lin YS, Ha I, Maldonado E, Reinberg D, Green MR. Binding of general transcription factor TFIIB to an acidic activating region. Nature. 1991 Oct 10;353(6344):569–571. [PubMed] [Google Scholar]
  • Liu F, Green MR. A specific member of the ATF transcription factor family can mediate transcription activation by the adenovirus E1a protein. Cell. 1990 Jun 29;61(7):1217–1224. [PubMed] [Google Scholar]
  • Lubahn DB, Joseph DR, Sar M, Tan J, Higgs HN, Larson RE, French FS, Wilson EM. The human androgen receptor: complementary deoxyribonucleic acid cloning, sequence analysis and gene expression in prostate. Mol Endocrinol. 1988 Dec;2(12):1265–1275. [PubMed] [Google Scholar]
  • Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM. Nuclear receptor that identifies a novel retinoic acid response pathway. Nature. 1990 May 17;345(6272):224–229. [PubMed] [Google Scholar]
  • Meyer ME, Gronemeyer H, Turcotte B, Bocquel MT, Tasset D, Chambon P. Steroid hormone receptors compete for factors that mediate their enhancer function. Cell. 1989 May 5;57(3):433–442. [PubMed] [Google Scholar]
  • Miesfeld R, Rusconi S, Godowski PJ, Maler BA, Okret S, Wikström AC, Gustafsson JA, Yamamoto KR. Genetic complementation of a glucocorticoid receptor deficiency by expression of cloned receptor cDNA. Cell. 1986 Aug 1;46(3):389–399. [PubMed] [Google Scholar]
  • Milbrandt J. Nerve growth factor induces a gene homologous to the glucocorticoid receptor gene. Neuron. 1988 May;1(3):183–188. [PubMed] [Google Scholar]
  • Miyajima N, Kadowaki Y, Fukushige S, Shimizu S, Semba K, Yamanashi Y, Matsubara K, Toyoshima K, Yamamoto T. Identification of two novel members of erbA superfamily by molecular cloning: the gene products of the two are highly related to each other. Nucleic Acids Res. 1988 Dec 9;16(23):11057–11074. [PMC free article] [PubMed] [Google Scholar]
  • Miyajima N, Horiuchi R, Shibuya Y, Fukushige S, Matsubara K, Toyoshima K, Yamamoto T. Two erbA homologs encoding proteins with different T3 binding capacities are transcribed from opposite DNA strands of the same genetic locus. Cell. 1989 Apr 7;57(1):31–39. [PubMed] [Google Scholar]
  • Mlodzik M, Hiromi Y, Weber U, Goodman CS, Rubin GM. The Drosophila seven-up gene, a member of the steroid receptor gene superfamily, controls photoreceptor cell fates. Cell. 1990 Jan 26;60(2):211–224. [PubMed] [Google Scholar]
  • Muñoz A, Zenke M, Gehring U, Sap J, Beug H, Vennström B. Characterization of the hormone-binding domain of the chicken c-erbA/thyroid hormone receptor protein. EMBO J. 1988 Jan;7(1):155–159. [PMC free article] [PubMed] [Google Scholar]
  • Nagpal S, Saunders M, Kastner P, Durand B, Nakshatri H, Chambon P. Promoter context- and response element-dependent specificity of the transcriptional activation and modulating functions of retinoic acid receptors. Cell. 1992 Sep 18;70(6):1007–1019. [PubMed] [Google Scholar]
  • Nagpal S, Friant S, Nakshatri H, Chambon P. RARs and RXRs: evidence for two autonomous transactivation functions (AF-1 and AF-2) and heterodimerization in vivo. EMBO J. 1993 Jun;12(6):2349–2360. [PMC free article] [PubMed] [Google Scholar]
  • Nakai A, Kartha S, Sakurai A, Toback FG, DeGroot LJ. A human early response gene homologous to murine nur77 and rat NGFI-B, and related to the nuclear receptor superfamily. Mol Endocrinol. 1990 Oct;4(10):1438–1443. [PubMed] [Google Scholar]
  • Nauber U, Pankratz MJ, Kienlin A, Seifert E, Klemm U, Jäckle H. Abdominal segmentation of the Drosophila embryo requires a hormone receptor-like protein encoded by the gap gene knirps. Nature. 1988 Dec 1;336(6198):489–492. [PubMed] [Google Scholar]
  • Ohno CK, Petkovich M. FTZ-F1 beta, a novel member of the Drosophila nuclear receptor family. Mech Dev. 1993 Jan;40(1-2):13–24. [PubMed] [Google Scholar]
  • Oro AE, Ong ES, Margolis JS, Posakony JW, McKeown M, Evans RM. The Drosophila gene knirps-related is a member of the steroid-receptor gene superfamily. Nature. 1988 Dec 1;336(6198):493–496. [PubMed] [Google Scholar]
  • Oro AE, McKeown M, Evans RM. Relationship between the product of the Drosophila ultraspiracle locus and the vertebrate retinoid X receptor. Nature. 1990 Sep 20;347(6290):298–301. [PubMed] [Google Scholar]
  • Pignoni F, Baldarelli RM, Steingrímsson E, Diaz RJ, Patapoutian A, Merriam JR, Lengyel JA. The Drosophila gene tailless is expressed at the embryonic termini and is a member of the steroid receptor superfamily. Cell. 1990 Jul 13;62(1):151–163. [PubMed] [Google Scholar]
  • Ptashne M, Gann AA. Activators and targets. Nature. 1990 Jul 26;346(6282):329–331. [PubMed] [Google Scholar]
  • Pugh BF, Tjian R. Mechanism of transcriptional activation by Sp1: evidence for coactivators. Cell. 1990 Jun 29;61(7):1187–1197. [PubMed] [Google Scholar]
  • Roeder RG. The complexities of eukaryotic transcription initiation: regulation of preinitiation complex assembly. Trends Biochem Sci. 1991 Nov;16(11):402–408. [PubMed] [Google Scholar]
  • Rothe M, Nauber U, Jäckle H. Three hormone receptor-like Drosophila genes encode an identical DNA-binding finger. EMBO J. 1989 Oct;8(10):3087–3094. [PMC free article] [PubMed] [Google Scholar]
  • Ryseck RP, Macdonald-Bravo H, Mattéi MG, Ruppert S, Bravo R. Structure, mapping and expression of a growth factor inducible gene encoding a putative nuclear hormonal binding receptor. EMBO J. 1989 Nov;8(11):3327–3335. [PMC free article] [PubMed] [Google Scholar]
  • Saatcioglu F, Bartunek P, Deng T, Zenke M, Karin M. A conserved C-terminal sequence that is deleted in v-ErbA is essential for the biological activities of c-ErbA (the thyroid hormone receptor). Mol Cell Biol. 1993 Jun;13(6):3675–3685. [PMC free article] [PubMed] [Google Scholar]
  • Saatcioglu F, Deng T, Karin M. A novel cis element mediating ligand-independent activation by c-ErbA: implications for hormonal regulation. Cell. 1993 Dec 17;75(6):1095–1105. [PubMed] [Google Scholar]
  • Sadowski I, Ptashne M. A vector for expressing GAL4(1-147) fusions in mammalian cells. Nucleic Acids Res. 1989 Sep 25;17(18):7539–7539. [PMC free article] [PubMed] [Google Scholar]
  • Sagami I, Tsai SY, Wang H, Tsai MJ, O'Malley BW. Identification of two factors required for transcription of the ovalbumin gene. Mol Cell Biol. 1986 Dec;6(12):4259–4267. [PMC free article] [PubMed] [Google Scholar]
  • Sap J, Muñoz A, Damm K, Goldberg Y, Ghysdael J, Leutz A, Beug H, Vennström B. The c-erb-A protein is a high-affinity receptor for thyroid hormone. Nature. 1986 Dec 18;324(6098):635–640. [PubMed] [Google Scholar]
  • Sap J, Muñoz A, Schmitt J, Stunnenberg H, Vennström B. Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene product. Nature. 1989 Jul 20;340(6230):242–244. [PubMed] [Google Scholar]
  • Schmitt J, Stunnenberg HG. The glucocorticoid receptor hormone binding domain mediates transcriptional activation in vitro in the absence of ligand. Nucleic Acids Res. 1993 Jun 11;21(11):2673–2681. [PMC free article] [PubMed] [Google Scholar]
  • Schöler HR, Ciesiolka T, Gruss P. A nexus between Oct-4 and E1A: implications for gene regulation in embryonic stem cells. Cell. 1991 Jul 26;66(2):291–304. [PubMed] [Google Scholar]
  • Segraves WA, Hogness DS. The E75 ecdysone-inducible gene responsible for the 75B early puff in Drosophila encodes two new members of the steroid receptor superfamily. Genes Dev. 1990 Feb;4(2):204–219. [PubMed] [Google Scholar]
  • Sladek FM, Zhong WM, Lai E, Darnell JE., Jr Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily. Genes Dev. 1990 Dec;4(12B):2353–2365. [PubMed] [Google Scholar]
  • Smith DP, Mason CS, Jones EA, Old RW. A novel nuclear receptor superfamily member in Xenopus that associates with RXR, and shares extensive sequence similarity to the mammalian vitamin D3 receptor. Nucleic Acids Res. 1994 Jan 11;22(1):66–71. [PMC free article] [PubMed] [Google Scholar]
  • Smith SE, Bohmann D. Functional dissection of AP-1 transcription factors using the Gal4 adaptor assay. Cell Growth Differ. 1992 Aug;3(8):523–529. [PubMed] [Google Scholar]
  • Stone BL, Thummel CS. The Drosophila 78C early late puff contains E78, an ecdysone-inducible gene that encodes a novel member of the nuclear hormone receptor superfamily. Cell. 1993 Oct 22;75(2):307–320. [PubMed] [Google Scholar]
  • Stunnenberg HG. Mechanisms of transactivation by retinoic acid receptors. Bioessays. 1993 May;15(5):309–315. [PubMed] [Google Scholar]
  • Tasset D, Tora L, Fromental C, Scheer E, Chambon P. Distinct classes of transcriptional activating domains function by different mechanisms. Cell. 1990 Sep 21;62(6):1177–1187. [PubMed] [Google Scholar]
  • Toney JH, Wu L, Summerfield AE, Sanyal G, Forman BM, Zhu J, Samuels HH. Conformational changes in chicken thyroid hormone receptor alpha 1 induced by binding to ligand or to DNA. Biochemistry. 1993 Jan 12;32(1):2–6. [PubMed] [Google Scholar]
  • Tora L, White J, Brou C, Tasset D, Webster N, Scheer E, Chambon P. The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell. 1989 Nov 3;59(3):477–487. [PubMed] [Google Scholar]
  • Tsai SY, Sagami I, Wang H, Tsai MJ, O'Malley BW. Interactions between a DNA-binding transcription factor (COUP) and a non-DNA binding factor (S300-II). Cell. 1987 Aug 28;50(5):701–709. [PubMed] [Google Scholar]
  • Tsukiyama T, Ueda H, Hirose S, Niwa O. Embryonal long terminal repeat-binding protein is a murine homolog of FTZ-F1, a member of the steroid receptor superfamily. Mol Cell Biol. 1992 Mar;12(3):1286–1291. [PMC free article] [PubMed] [Google Scholar]
  • Vegeto E, Allan GF, Schrader WT, Tsai MJ, McDonnell DP, O'Malley BW. The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor. Cell. 1992 May 15;69(4):703–713. [PubMed] [Google Scholar]
  • Vivanco Ruiz MM, Bugge TH, Hirschmann P, Stunnenberg HG. Functional characterization of a natural retinoic acid responsive element. EMBO J. 1991 Dec;10(12):3829–3838. [PMC free article] [PubMed] [Google Scholar]
  • Wang LH, Tsai SY, Cook RG, Beattie WG, Tsai MJ, O'Malley BW. COUP transcription factor is a member of the steroid receptor superfamily. Nature. 1989 Jul 13;340(6229):163–166. [PubMed] [Google Scholar]
  • Webster NJ, Green S, Jin JR, Chambon P. The hormone-binding domains of the estrogen and glucocorticoid receptors contain an inducible transcription activation function. Cell. 1988 Jul 15;54(2):199–207. [PubMed] [Google Scholar]
  • Weigel NL, Beck CA, Estes PA, Prendergast P, Altmann M, Christensen K, Edwards DP. Ligands induce conformational changes in the carboxyl-terminus of progesterone receptors which are detected by a site-directed antipeptide monoclonal antibody. Mol Endocrinol. 1992 Oct;6(10):1585–1597. [PubMed] [Google Scholar]
  • Weinberger C, Thompson CC, Ong ES, Lebo R, Gruol DJ, Evans RM. The c-erb-A gene encodes a thyroid hormone receptor. Nature. 1986 Dec 18;324(6098):641–646. [PubMed] [Google Scholar]
  • Weinzierl RO, Dynlacht BD, Tjian R. Largest subunit of Drosophila transcription factor IID directs assembly of a complex containing TBP and a coactivator. Nature. 1993 Apr 8;362(6420):511–517. [PubMed] [Google Scholar]
  • Weiss RE, Refetoff S. Thyroid hormone resistance. Annu Rev Med. 1992;43:363–375. [PubMed] [Google Scholar]
  • Zawel L, Reinberg D. Advances in RNA polymerase II transcription. Curr Opin Cell Biol. 1992 Jun;4(3):488–495. [PubMed] [Google Scholar]
  • Zenke M, Muñoz A, Sap J, Vennström B, Beug H. v-erbA oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA. Cell. 1990 Jun 15;61(6):1035–1049. [PubMed] [Google Scholar]
  • Zhou Q, Lieberman PM, Boyer TG, Berk AJ. Holo-TFIID supports transcriptional stimulation by diverse activators and from a TATA-less promoter. Genes Dev. 1992 Oct;6(10):1964–1974. [PubMed] [Google Scholar]
Articles from The EMBO Journal are provided here courtesy of Nature Publishing Group
-