54
Views
37
CrossRef citations to date
0
Altmetric
Transcriptional Regulation

Characterization of the DNA-Binding and Dimerization Properties of the Nuclear Orphan Receptor Germ Cell Nuclear Factor

, , , , &
Pages 690-703 | Received 13 Jul 1998, Accepted 19 Oct 1998, Published online: 28 Mar 2023

REFERENCES

  • Achatz, G., B. Holzl, R. Speckmayer, C. Hauser, F. Sandhofer, and J. Paulweber 1997. Functional domains of the human orphan receptor ARP-1/COUP-TFII involved in active repression and transrepression. Mol. Cell. Biol. 17:4914–4932.
  • Barettino, D., M. M. Vivanco Ruiz, and J. Stunnenberg 1994. Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor. EMBO J. 13:3039–3049.
  • Beato, M., P. Herrlich, and J. Schütz 1995. Steroid hormone receptors: many actors in search of a plot. Cell 83:851–857.
  • Borgmeyer, U. 1997. Dimeric binding of the mouse germ cell nuclear factor. Eur. J. Biochem. 244:120–127.
  • Bourguet, W., M. Ruff, P. Chambon, H. Gronemeyer, and J. Moras 1995. Crystal structure of the ligand-binding domain of the human nuclear receptor RXRα. Nature 375:377–382.
  • Brzozowski, A. M., A. C. W. Pike, Z. Dauter, R. E. Hubbard, T. Bonn, O. Engström, L. Öhman, G. L. Greene, J.-A. Gustafsson, and J. Carlquist 1997. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature 389:753–758.
  • Chambon, P. 1996. A decade of molecular biology of retinoic acid receptors. FASEB J. 10:940–954.
  • Chen, F., A. J. Cooney, Y. Wang, S. W. Law, and J. O’Malley 1994. Cloning of a novel orphan receptor (GCNF) expressed during germ cell development. Mol. Endocrinol. 8:1434–1444.
  • Cooney, A. J., G. C. Hummelke, T. Herman, F. Chen, and J. Jackson 1998. Germ cell nuclear factor is a response element-specific repressor of transcription. Biochem. Biophys. Res. Commun. 245:94–100.
  • Danielian, P. S., R. White, J. A. Lees, and J. Parker 1992. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J. 11:1025–1033.
  • Durand, B., M. Saunders, C. Gaudon, B. Roy, R. Losson, and J. Chambon 1994. Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity. EMBO J. 13:5370–5382.
  • Evans, R. M. 1988. The steroid and thyroid hormone receptor superfamily. Science 240:889–895.
  • Geourjon, C., and J. Deleage 1995. SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput. Appl. Biosci. 11:681–684.
  • Glass, C. K., D. W. Rose, and J. Rosenfeld 1997. Nuclear receptor coactivators. Curr. Opin. Cell Biol. 9:222–232.
  • Greiner, E. F., J. Kirfel, H. Greschik, U. Dörflinger, P. Becker, A. Mercep, and J. Schüle 1996. Functional analysis of retinoid Z receptor β, a brain-specific nuclear orphan receptor. Proc. Natl. Acad. Sci. USA 93:10105–10110.
  • Gronemeyer, H., and J. Laudet 1995. Transcription factors 3: nuclear receptors. Protein Profile 2:1173–1308.
  • Gronemeyer, H., and J. Moras 1995. How to finger DNA. Nature 375:190–191.
  • Hirose, T., D. A. O’Brien, and J. Jetten 1995. RTR: a new member of the nuclear receptor superfamily that is highly expressed in murine testis. Gene 152:247–251.
  • Holmbeck, S. M. A., M. P. Foster, D. R. Casimiro, D. S. Sem, H. J. Dyson, and J. Wright 1998. High-resolution structure of the retinoid X receptor DNA-binding domain. J. Mol. Biol. 281:271–284.
  • Joos, T. O., R. David, and J. Dreyer 1996. xGCNF, a nuclear orphan receptor is expressed during neurulation in Xenopus laevis. Mech. Dev. 60:45–57.
  • Kapelle, M., J. Kratzschmar, M. Husemann, and J. Schleuning 1997. cDNA cloning of two closely related forms of human germ cell nuclear factor (GCNF). Biochim. Biophys. Acta 1352:13–17.
  • Katz, D., C. Niederberger, G. R. Slaughter, and J. Cooney 1997. Characterization of germ cell-specific expression of the orphan nuclear receptor, germ cell nuclear factor. Endocrinology 138:4364–4372.
  • Keidel, S., P. LeMotte, and J. Apfel 1994. Different agonist- and antagonist-induced conformational changes in retinoic acid receptors analyzed by protease mapping. Mol. Cell. Biol. 14:287–298.
  • Kurokawa, R., V. C. Yu, A. Naar, S. Kyakumoto, Z. Han, S. Silverman, M. G. Rosenfeld, and J. Glass 1993. Differential orientations of the DNA-binding domain and carboxy-terminal dimerization interface regulate binding site selection by nuclear receptor heterodimers. Genes Dev. 7:1423–1435.
  • Lee, M. S., S. A. Kliewer, J. Provencal, P. E. Wright, and J. Evans 1993. Structure of the retinoid X receptor α DNA binding domain: a helix required for homodimeric DNA binding. Science 260:1117–1121.
  • Lei, W., T. Hirose, L.-X. Zhang, H. Adachi, M. J. Spinella, E. Dmitrovsky, and J. Jetten 1997. Cloning of the human orphan receptor germ cell nuclear factor/retinoid receptor-related testis-associated receptor and its differential regulation during embryonal carcinoma cell differentiation. J. Mol. Endocrinol. 18:167–176.
  • Mangelsdorf, D. J., and J. Evans 1995. The RXR heterodimers and orphan receptors. Cell 83:841–850.
  • Mangelsdorf, D. J., C. Thummel, M. Beato, P. Herrlich, G. Schütz, K. Umesono, B. Blumberg, P. Kastner, M. Mark, P. Chambon, and J. Evans 1995. The nuclear receptor superfamily: the second decade. Cell 83:835–839.
  • Nicholls, A., K. A. Sharp, and J. Honig 1991. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11:281–296.
  • Perlmann, T., P. N. Rangarajan, K. Umesono, and J. Evans 1993. Determinants for selective RAR and TR recognition of direct repeat HREs. Genes Dev. 7:1411–1422.
  • Perlmann, T., K. Umesono, P. N. Rangarajan, B. M. Forman, and J. Evans 1996. Two distinct dimerization interfaces differentially modulate target gene specificity of nuclear hormone receptors. Mol. Endocrinol. 10:958–966.
  • Perlmann, T., and J. Evans 1997. Nuclear receptors in Sicily: all in the famiglia. Cell 90:391–397.
  • Pfitzner, E., P. Becker, A. Rolke, and J. Schüle 1995. Functional antagonism between the retinoic acid receptor and the viral transactivator BZLF1 is mediated by protein-protein interactions. Proc. Natl. Acad. Sci. USA 92:12265–12269.
  • Qi, J. S., V. Desai-Yajnik, M. E. Greene, B. M. Raaka, and J. Samuels 1995. The ligand-binding domains of the thyroid hormone/retinoid receptor gene subfamily function in vivo to mediate heterodimerization, gene silencing, and transactivation. Mol. Cell. Biol. 15:1817–1825.
  • Rastinejad, F., T. Perlmann, R. M. Evans, and J. Sigler 1995. Structural determinants for nuclear receptor assembly on DNA direct repeats. Nature 375:203–211.
  • Renaud, J.-P., N. Rochel, M. Ruff, V. Vivat, P. Chambon, H. Gronemeyer, and J. Moras 1995. Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. Nature 378:681–689.
  • Rost, B. 1996. PHD: predicting one-dimensional protein structure by profile-based neural networks. Methods Enzymol. 266:525–539.
  • Sali, A., and J. Blundell 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779–815.
  • Schwabe, J. W. R., L. Chapman, J. T. Finch, and J. Rhodes 1993. The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell 75:567–578.
  • Seol, W., M. Chung, and J. Moore 1997. Novel receptor interaction and repression domains in the orphan receptor SHP. Mol. Cell. Biol. 17:7126–7131.
  • Süsens, U., and J. Borgmeyer 1996. Characterization of the human germ cell nuclear factor gene. Biochim. Biophys. Acta 1309:179–182.
  • Trapp, T., and J. Holsboer 1995. Ligand-induced conformational changes of the mineralcorticoid receptor analyzed by protease mapping. Biochem. Biophys. Res. Commun. 215:286–291.
  • Umesono, K., K. K. Murakami, C. C. Thompson, and J. Evans 1991. Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptors. Cell 65:1255–1266.
  • Vivat, V., C. Zechel, J.-M. Wurtz, W. Bourguet, H. Kagechika, H. Umemiya, K. Shudo, D. Moras, H. Gronemeyer, and J. Chambon 1997. A mutation mimicking ligand-induced conformational change yields a constitutive RXR that senses allosteric effects in heterodimers. EMBO J. 16:5697–5709.
  • Wagner, R. L., J. W. Apriletti, M. E. McGrath, B. L. West, J. D. Baxter, and J. Fletterick 1995. A structural role for hormone in the thyroid hormone receptor. Nature 378:690–697.
  • Weis, K. E., K. Ekena, J. A. Thomas, G. Lazennec, and J. Katzenellenbogen 1996. Constitutively active human estrogen receptors containing amino acid substitutions for tyrosine 537 in the receptor protein. Mol. Endocrinol. 10:1388–1398.
  • White, R., M. Sjöberg, E. Kalkhooven, and J. Parker 1997. Ligand independent activation of the oestrogen receptor by mutation of a conserved tyrosine. EMBO J. 16:1427–1435.
  • Wilson, T. E., R. E. Paulsen, K. A. Padgett, and J. Milbrandt 1992. Participation of non zinc-finger residues in DNA binding by two nuclear orphan receptors. Science 256:107–110.
  • Wilson, T. E., T. J. Fahrner, and J. Milbrandt 1993. The orphan receptors NGFI-B and steroidogenic factor 1 establish monomer binding as the third paradigm of nuclear receptor-DNA interaction. Mol. Cell. Biol. 13:5794–5804.
  • Wurtz, J.-M., W. Bourguet, J.-P. Renaud, V. Vivat, P. Chambon, D. Moras, and J. Gronemeyer 1996. A canonical structure for the ligand-binding domain of nuclear receptors. Nat. Struct. Biol. 3:87–94.
  • Yan, Z. H., A. Medvedev, T. Hirose, H. Gotoh, and J. Jetten 1997. Characterization of the response element and DNA binding properties of the nuclear orphan receptor germ cell nuclear factor/retinoid receptor-related testis-associated receptor. J. Biol. Chem. 272:10565–10572.
  • Zechel, C., X. Q. Shen, P. Chambon, and J. Gronemeyer 1994. Dimerization interfaces formed between the DNA binding domains determine the cooperative binding of RXR/RAR and RXR/TR heterodimers to DR5 and DR4 elements. EMBO J. 13:1414–1424.
  • Zechel, C., X. Q. Shen, J. Y. Chen, Z. P. Chen, P. Chambon, and J. Gronemeyer 1994. The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full-length receptors to direct repeats. EMBO J. 13:1425–1433.
  • Zhang, X. K., J. Lehmann, B. Hoffmann, M. Dawson, J. Cameron, G. Graupner, T. Hermann, P. Tran, and J. Pfahl 1992. Homodimer formation of retinoid X receptor induced by 9-cis retinoic acid. Nature 358:587–591.
  • Zhang, X. K., G. Salbert, M. O. Lee, and J. Pfahl 1994. Mutations that alter ligand-induced switches and dimerization activities in the retinoid X receptor. Mol. Cell. Biol. 14:4311–4323.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.