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. 1986 Dec;83(23):9045–9049. doi: 10.1073/pnas.83.23.9045

Cloning and sequence analysis of rabbit progesterone-receptor complementary DNA.

H Loosfelt, M Atger, M Misrahi, A Guiochon-Mantel, C Meriel, F Logeat, R Benarous, E Milgrom
PMCID: PMC387071  PMID: 3538016

Abstract

Two lambda gt11 clones containing fragments of cDNA encoding the rabbit progesterone receptor were isolated with the aid of monoclonal and monospecific polyclonal antireceptor antibodies. RNA gel blot analysis showed that the corresponding mRNA was approximately equal to 5900 nucleotides in size and present in the uterus, where its concentration was increased by estrogen treatment, and in the vagina. This mRNA was not detected in liver, in spleen, in intestine, and in kidney where the receptor protein is known to be absent or present in very small concentration. Cross-hybridizing clones were isolated from a lambda 10 library. The DNA was sequenced, and the primary structure of the progesterone receptor was deduced. It consists of 930 amino acids and contains a basic, cysteine-rich region (residues 568-645) with extensive homology to the glucocorticoid and estrogen receptors and the v-erbA oncogene protein. This region is followed by a C-terminal domain that is similar in size to the corresponding domains of the other steroid receptors and v-erbA and shows striking amino acid homology with the glucocorticoid receptor and significant homology with the estrogen receptor. In contrast, the region extending from the cysteine-rich segment toward the N terminus differed in size and amino acid sequence from that of the other receptors and v-erbA. This region had a high proline content in the progesterone receptor.

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Selected References

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  1. Debuire B., Henry C., Bernissa M., Biserte G., Claverie J. M., Saule S., Martin P., Stehelin D. Sequencing the erbA gene of avian erythroblastosis virus reveals a new type of oncogene. Science. 1984 Jun 29;224(4656):1456–1459. doi: 10.1126/science.6328658. [DOI] [PubMed] [Google Scholar]
  2. Green S., Walter P., Kumar V., Krust A., Bornert J. M., Argos P., Chambon P. Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature. 1986 Mar 13;320(6058):134–139. doi: 10.1038/320134a0. [DOI] [PubMed] [Google Scholar]
  3. Greene G. L., Gilna P., Waterfield M., Baker A., Hort Y., Shine J. Sequence and expression of human estrogen receptor complementary DNA. Science. 1986 Mar 7;231(4742):1150–1154. doi: 10.1126/science.3753802. [DOI] [PubMed] [Google Scholar]
  4. Greene G. L., Nolan C., Engler J. P., Jensen E. V. Monoclonal antibodies to human estrogen receptor. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5115–5119. doi: 10.1073/pnas.77.9.5115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
  6. Hall M. N., Hereford L., Herskowitz I. Targeting of E. coli beta-galactosidase to the nucleus in yeast. Cell. 1984 Apr;36(4):1057–1065. doi: 10.1016/0092-8674(84)90055-2. [DOI] [PubMed] [Google Scholar]
  7. Hathaway G. M., Traugh J. A. Casein kinases--multipotential protein kinases. Curr Top Cell Regul. 1982;21:101–127. [PubMed] [Google Scholar]
  8. Hollenberg S. M., Weinberger C., Ong E. S., Cerelli G., Oro A., Lebo R., Thompson E. B., Rosenfeld M. G., Evans R. M. Primary structure and expression of a functional human glucocorticoid receptor cDNA. Nature. 1985 Dec 19;318(6047):635–641. doi: 10.1038/318635a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hubbard S. C., Ivatt R. J. Synthesis and processing of asparagine-linked oligosaccharides. Annu Rev Biochem. 1981;50:555–583. doi: 10.1146/annurev.bi.50.070181.003011. [DOI] [PubMed] [Google Scholar]
  10. Kalderon D., Roberts B. L., Richardson W. D., Smith A. E. A short amino acid sequence able to specify nuclear location. Cell. 1984 Dec;39(3 Pt 2):499–509. doi: 10.1016/0092-8674(84)90457-4. [DOI] [PubMed] [Google Scholar]
  11. Kamps M. P., Taylor S. S., Sefton B. M. Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent protein kinase have homologous ATP-binding sites. Nature. 1984 Aug 16;310(5978):589–592. doi: 10.1038/310589a0. [DOI] [PubMed] [Google Scholar]
  12. Kozak M. Point mutations close to the AUG initiator codon affect the efficiency of translation of rat preproinsulin in vivo. Nature. 1984 Mar 15;308(5956):241–246. doi: 10.1038/308241a0. [DOI] [PubMed] [Google Scholar]
  13. Krebs E. G., Beavo J. A. Phosphorylation-dephosphorylation of enzymes. Annu Rev Biochem. 1979;48:923–959. doi: 10.1146/annurev.bi.48.070179.004423. [DOI] [PubMed] [Google Scholar]
  14. Krust A., Green S., Argos P., Kumar V., Walter P., Bornert J. M., Chambon P. The chicken oestrogen receptor sequence: homology with v-erbA and the human oestrogen and glucocorticoid receptors. EMBO J. 1986 May;5(5):891–897. doi: 10.1002/j.1460-2075.1986.tb04300.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Laughon A., Scott M. P. Sequence of a Drosophila segmentation gene: protein structure homology with DNA-binding proteins. Nature. 1984 Jul 5;310(5972):25–31. doi: 10.1038/310025a0. [DOI] [PubMed] [Google Scholar]
  16. Logeat F., Hai M. T., Milgrom E. Antibodies to rabbit progesterone receptor: crossreaction with human receptor. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1426–1430. doi: 10.1073/pnas.78.3.1426. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Logeat F., Pamphile R., Loosfelt H., Jolivet A., Fournier A., Milgrom E. One-step immunoaffinity purification of active progesterone receptor. Further evidence in favor of the existence of a single steroid binding subunit. Biochemistry. 1985 Feb 12;24(4):1029–1035. doi: 10.1021/bi00325a034. [DOI] [PubMed] [Google Scholar]
  18. Logeat F., Vu Hai M. T., Fournier A., Legrain P., Buttin G., Milgrom E. Monoclonal antibodies to rabbit progesterone receptor: crossreaction with other mammalian progesterone receptors. Proc Natl Acad Sci U S A. 1983 Nov;80(21):6456–6459. doi: 10.1073/pnas.80.21.6456. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Loosfelt H., Logeat F., Vu Hai M. T., Milgrom E. The rabbit progesterone receptor. Evidence for a single steroid-binding subunit and characterization of receptor mRNA. J Biol Chem. 1984 Nov 25;259(22):14196–14202. [PubMed] [Google Scholar]
  20. Miesfeld R., Okret S., Wikström A. C., Wrange O., Gustafsson J. A., Yamamoto K. R. Characterization of a steroid hormone receptor gene and mRNA in wild-type and mutant cells. Nature. 1984 Dec 20;312(5996):779–781. doi: 10.1038/312779a0. [DOI] [PubMed] [Google Scholar]
  21. Okret S., Wikström A. C., Wrange O., Andersson B., Gustafsson J. A. Monoclonal antibodies against the rat liver glucocorticoid receptor. Proc Natl Acad Sci U S A. 1984 Mar;81(6):1609–1613. doi: 10.1073/pnas.81.6.1609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Patschinsky T., Hunter T., Esch F. S., Cooper J. A., Sefton B. M. Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation. Proc Natl Acad Sci U S A. 1982 Feb;79(4):973–977. doi: 10.1073/pnas.79.4.973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Perrot-Applanat M., Groyer-Picard M. T., Logeat F., Milgrom E. Ultrastructural localization of the progesterone receptor by an immunogold method: effect of hormone administration. J Cell Biol. 1986 Apr;102(4):1191–1199. doi: 10.1083/jcb.102.4.1191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Perrot-Applanat M., Logeat F., Groyer-Picard M. T., Milgrom E. Immunocytochemical study of mammalian progesterone receptor using monoclonal antibodies. Endocrinology. 1985 Apr;116(4):1473–1484. doi: 10.1210/endo-116-4-1473. [DOI] [PubMed] [Google Scholar]
  25. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Thomas P. S. Hybridization of denatured RNA transferred or dotted nitrocellulose paper. Methods Enzymol. 1983;100:255–266. doi: 10.1016/0076-6879(83)00060-9. [DOI] [PubMed] [Google Scholar]
  27. Walter P., Green S., Greene G., Krust A., Bornert J. M., Jeltsch J. M., Staub A., Jensen E., Scrace G., Waterfield M. Cloning of the human estrogen receptor cDNA. Proc Natl Acad Sci U S A. 1985 Dec;82(23):7889–7893. doi: 10.1073/pnas.82.23.7889. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Weinberger C., Hollenberg S. M., Ong E. S., Harmon J. M., Brower S. T., Cidlowski J., Thompson E. B., Rosenfeld M. G., Evans R. M. Identification of human glucocorticoid receptor complementary DNA clones by epitope selection. Science. 1985 May 10;228(4700):740–742. doi: 10.1126/science.2581314. [DOI] [PubMed] [Google Scholar]
  29. Weinberger C., Hollenberg S. M., Rosenfeld M. G., Evans R. M. Domain structure of human glucocorticoid receptor and its relationship to the v-erb-A oncogene product. Nature. 1985 Dec 19;318(6047):670–672. doi: 10.1038/318670a0. [DOI] [PubMed] [Google Scholar]
  30. Westphal H. M., Moldenhauer G., Beato M. Monoclonal antibodies to the rat liver glucocorticoid receptor. EMBO J. 1982;1(11):1467–1471. doi: 10.1002/j.1460-2075.1982.tb01339.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Zarucki-Schulz T., Kulomaa M. S., Headon D. R., Weigel N. L., Baez M., Edwards D. P., McGuire W. L., Schrader W. T., O'Malley B. W. Molecular cloning of a cDNA for the chicken progesterone receptor B antigen. Proc Natl Acad Sci U S A. 1984 Oct;81(20):6358–6362. doi: 10.1073/pnas.81.20.6358. [DOI] [PMC free article] [PubMed] [Google Scholar]

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