Functional properties of the N-terminal region of progesterone receptors and their mechanistic relationship to structure

Journal of Steroid Biochemistry and Molecular Biology

Volumn 85, Issue 2-5, 2003, Pages 209-219

  Takimoto, Glenn S ^a   Tung, Lin ^a   Abdel Hafiz, Hany ^a   Abel, Michael G ^a   Sartorius, Carol A ^a   Richer, Jennifer K ^a   Jacobsen, Britta M ^a   Bain, David L ^a   Horwitz, Kathryn B ^a  

^a UNIVERSITY OF COLORADO   (United States)

Author keywords

Activation domain; Cofactors; Progesterone receptor; Repression; Structure; SUMO; Synergism; Transcription

Indexed keywords

DNA; GLUCOCORTICOID; PROGESTERONE RECEPTOR; SUMO 1 PROTEIN;

AMINO TERMINAL SEQUENCE; ATTENUATION; BIOCHEMISTRY; BIOPHYSICS; CONFERENCE PAPER; DNA BINDING; DNA STRUCTURE; ENZYME ACTIVITY; HORMONE STRUCTURE; HUMAN; NONHUMAN; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; TRANSACTIVATION;

EID: 0042889510     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-0760(03)00197-3     Document Type: Conference Paper

References (38)

1. Evans R.M. The steroid and thyroid hormone receptor superfamily. Science. 240(4854):1988;889-895.
2. He B., Lee L.W., Minges J.T., Wilson E.M. Dependence of selective gene activation on the androgen receptor NH2- and COOH-terminal interaction. J. Biol. Chem. 277(28):2002;25631-25639.
3. Tung L., Shen T., Abel M.G., Powell R.L., Takimoto G.S., Sartorius C.A., Horwitz K.B. Mapping the unique activation function 3 in the progesterone B-receptor upstream segment. Two LXXLL motifs and a tryptophan residue are required for activity. J. Biol. Chem. 276(43):2002;39843-39851.
4. Abdel-Hafiz H., Takimoto G.S., Tung L., Horwitz K.B. The inhibitory function in human progesterone receptor N termini binds SUMO-1 protein to regulate autoinhibition and transrepression. J. Biol. Chem. 277(37):2002;33950-33956.
5. Bain D.L., Franden M.A., McManaman J.L., Takimoto G.S., Horwitz K.B. The N-terminal region of the human progesterone A-receptor. Structural analysis and the influence of the DNA binding domain. J. Biol. Chem. 275(10):2000;7313-7320.
6. Bain D.L., Franden M.A., McManaman J.L., Takimoto G.S., Horwitz K.B. The N-terminal region of human progesterone B-receptors: biophysical and biochemical comparison to A-receptors. J. Biol. Chem. 276(26):2001;23825-23831.
7. Kumar R., Thompson E.B. Transactivation functions of the N-terminal domains of nuclear hormone receptors: protein folding and coactivator interactions. Mol. Endocrinol. 17(1):2003;1-10.
8. Sartorius C.A., Melville M.Y., Hovland A.R., Tung L., Takimoto G.S., Horwitz K.B. A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B-isoform. Mol. Endocrinol. 8(10):1994;1347-1360.
9. Hovland A.R., Powell R.L., Takimoto G.S., Tung L., Horwitz K.B. An N-terminal inhibitory function, IF, suppresses transcription by the A-isoform but not the B-isoform of human progesterone receptors. J. Biol. Chem. 273(10):1998;5455-5460.
10. Giangrande P.H., Pollio G., McDonnell D.P. Mapping and characterization of the functional domains responsible for the differential activity of the A and B isoforms of the human progesterone receptor. J. Biol. Chem. 272(52):1997;32889-32900.
11. Huse B., Verca S.B., Matthey P., Rusconi S. Definition of a negative modulation domain in the human progesterone receptor. Mol. Endocrinol. 12(9):1998;1334-1342.
12. Meyer M.E., Pornon A., Ji J.W., Bocquel M.T., Chambon P., Gronemeyer H. Agonistic and antagonistic activities of RU486 on the functions of the human progesterone receptor. EMBO J. 9(12):1990;3923-3932.
13. Tung L., Mohamed M.K., Hoeffler J.P., Takimoto G.S., Horwitz K.B. Antagonist-occupied human progesterone B-receptors activate transcription without binding to progesterone response elements and are dominantly inhibited by A-receptors. Mol. Endocrinol. 7(10):1993;1256-1265.
14. Giangrande P.H., Kimbrel E.A., Edwards D.P., McDonnell D.P. The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding. Mol. Cell. Biol. 20(9):2000;3102-3115.
15. Richer J.K., Jacobsen B.M., Manning N.G., Abel M.G., Wolf D.M., Horwitz K.B. Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells. J. Biol. Chem. 277(7):2002;5209-5218.
16. Jacobsen B.M., Richer J.K., Schittone S.A., Horwitz K.B. New human breast cancer cells to study progesterone receptor isoform ratio effects and ligand-independent gene regulation. J. Biol. Chem. 277(31):2002;27793-27800.
17. Poukka H., Karvonen U., Janne O.A., Palvimo J.J. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. U.S.A. 97(26):2000;14145-14150.
18. Iniguez-Lluhi J.A., Pearce D. A common motif within the negative regulatory regions of multiple factors inhibits their transcriptional synergy. Mol. Cell. Biol. 20(16):2000;6040-6050.
19. Winkley C.S., Keller M.J., Jaehning J.A. A multicomponent mitochondrial RNA polymerase from Saccharomyces cerevisiae. J. Biol. Chem. 260(26):1985;14214-14223.
20. Gietz R.D., Sugino A. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six base pair restriction sites. Gene. 74(2):1988;527-534.
21. Muhlrad D., Hunter R., Parker R. A rapid method for localized mutagenesis of yeast genes. Yeast. 8(2):1992;79-82.
22. Gietz R.D. Transforming yeast with DNA. Methods Mol. Cell. Biol. 5:1995;255-269.
23. Bohen S.P., Yamamoto K.R. Isolation of Hsp90 mutants by screening for decreased steriod receptor function. Proc. Natl. Acad. Sci. U.S.A. 90(23):1993;11424-11428.
24. Hard T., Kellenbach E., Boelens R., Maler B.A., Dahlman K., Freedman L.P., Carlstedt-Duke J., Yamamoto K.R., Gustafsson J.A., Kaptein R. Solution structure of the glucocorticoid receptor DNA-binding domain. Science. 249(4965):1990;157-160.
25. Guiochon-Mantel A., Loosfelt H., Lescop P., Sar S., Atger M., Perrot-Applanat M., Milgrom E. Mechanisms of nuclear localization of the progesterone receptor: evidence for interaction between monomers. Cell. 57(7):1989;1147-1154.
26. Simental J.A., Sar M., Lane M.V., French F.S., Wilson E.M. Transcriptional activation and nuclear targeting signals of the human androgen receptor. J. Biol. Chem. 266(1):1991;510-518.
27. Onate S.A., Boonyaratanakornkit V., Spencer T.E., Tsai S.Y., Tsai M.J., Edwards D.P., O'Malley B.W. The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors. J. Biol. Chem. 273(20):1998;12101-12118.
28. Kumar R., Lee J.C., Bolen D.W., Thompson E.B. The conformation of the glucocorticoid receptor af1/tau1 domain induced by osmolyte binds co-regulatory proteins. J. Biol. Chem. 276(21):2001;18146-18152.
29. Ikonen T., Palvimo J.J., Janne O.A. Interaction between the amino- and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators. J. Biol. Chem. 272(47):1997;29821-29828.
30. Metivier R., Penot G., Flouriot G., Pakdel F. Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains. Mol. Endocrinol. 15(11):2001;1953-1970.
31. Kumar R., Baskakov I.V., Srinivasan G., Bolen D.W., Lee J.C., Thompson E.B. Interdomain signaling in a two-domain fragment of the human glucocorticoid receptor. J. Biol. Chem. 274(35):1999;24737-24741.
32. Tetel M.J., Giangrande P.H., Leonhardt S.A., McDonnell D.P., Edwards D.P. Hormone-dependent interaction between the amino- and carboxyl-terminal domains of progesterone receptor in vitro and in vivo. Mol. Endocrinol. 13(6):1999;910-924.
33. Warnmark A., Gustafsson J.A., Wright A.P. Architectural principles for the structure and function of the glucocorticoid receptor tau 1 core activation domain. J. Biol. Chem. 275(20):2000;15014-15018.
34. Dahlman-Wright K., Baumann H., McEwan I.J., Almlof T., Wright A.P., Gustafsson J.A., Hard T. Structural characterization of a minimal functional transactivation domain from the human glucocorticoid receptor. Proc. Natl. Acad. Sci. U.S.A. 92(5):1995;1699-1703.
35. Warnmark A., Wikstrom A., Wright A.P., Gustafsson J.A., Hard T. The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. J. Biol. Chem. 276(49):2001;45939-45944.
36. Reid J., Kelly S.M., Watt K., Price N.C., McEwan I.J. Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. J. Biol. Chem. 277(22):2002;20079-20086.
37. Williams S.P., Sigler P.B. Atomic structure of progesterone complexed with its receptor. Nature. 393(6683):1998;392-396.
38. Jantzen H.M., Strahle U., Gloss B., Stewart F., Schmid W., Boshart M., Miksicek R., Schutz G. Cooperativity of glucocorticoid response elements located far upstream of the tyrosine aminotransferase gene. Cell. 49(1):1987;29-38.