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Molecular Endocrinology, Vol 8, 1347-1360, Copyright © 1994 by Endocrine Society

ARTICLES

A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B-isoform

CA Sartorius, MY Melville, AR Hovland, L Tung, GS Takimoto and KB Horwitz
Department of Medicine and Pathology, University of Colorado Health Sciences Center, Denver 80262.

Human progesterone target tissues contain two progesterone receptors: B- receptors (hPRB), which are 933 amino acids in length, and A-receptors (hPRA), which lack the N-terminal 164 amino acids. The two isoforms differ functionally when they are occupied by agonists or antagonists. We postulated that the unique 164-amino acid, B-upstream segment (BUS) is in part responsible for the functional differences between the two isoforms and have constructed a series of hPR expression vectors encoding BUS fused to isolated down-stream functional domains of the receptors. These include the two transactivation domains: activation function-1 (AF1), located in a 90-amino acid segment just up-stream of the DNA-binding domain (DBD) and nuclear localization signal (NLS), and AF2, located in the hormone-binding domain. BUS is a highly phosphorylated domain, and contains the serine residues responsible for the hPRB triplet protein structure. The construct containing BUS-DBD- NLS binds tightly to DNA when aided by accessory nuclear factors. In HeLa cells, BUS-DBD-NLS strongly and autonomously activates transcription of chloramphenicol acetyltransferase (CAT) from a promoter containing two progesterone response elements (PRE2-TATAtk- CAT). Transcription levels with BUS-DBD-NLS are equivalent to those seen with full-length hPRB, and are higher than those seen with hPRA. BUS specifically requires an intact hPR DBD to be transcriptionally active. DBD mutants that cannot bind DNA or whose DNA binding specificity has been switched to an estrogen response element cannot cooperate in BUS transcriptional activity. The function of BUS-DBD-NLS is promoter and cell specific. It does not transactivate a CAT reporter driven by the mouse mammary tumor virus promoter in HeLa cells and poorly transactivates PRE2-TATAtk-CAT in PR-negative T47D breast cancer cells. However, in the breast cancer cells, BUS-DBD-NLS transactivation of PRE2-TATAtk-CAT can be reconstituted by either elevating cellular levels of cAMP or linking BUS and DBD to AF1 or AF2 of hPR, each of which alone is also inactive in these cells. We conclude that hPRB contains a unique third activation function (AF3) located within BUS and requiring the functional DBD of hPR. Depending on the promoter or cell tested, AF3 can activate transcription autonomously, or it can functionally synergize with AF1 or AF2. Autonomous AF3 function may explain the unexpected transactivating actions of antiprogestin- occupied hPRB, an issue of importance in hormone-resistant breast cancers and in tissue-specific agonist-like effects of hormone antagonists.


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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., December 26, 1997; 272(52): 32889 - 32900.
[Abstract] [Full Text] [PDF]

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 Mol. Endocrinol.Home page
S. D. Groshong, G. I. Owen, B. Grimison, I. E. Schauer, M. C. Todd, T. A. Langan, R. A. Sclafani, C. A. Lange, and K. B. Horwitz
Biphasic Regulation of Breast Cancer Cell Growth by Progesterone: Role of the Cyclin-Dependent Kinase Inhibitors, p21 and p27Kip1
Mol. Endocrinol., October 1, 1997; 11(11): 1593 - 1607.
[Abstract] [Full Text]

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 Mol. Endocrinol.Home page
W. Gong, S. Chávez, and M. Beato
Point Mutation in the Ligand-Binding Domain of the Progesterone Receptor Generates a Transdominant Negative Phenotype
Mol. Endocrinol., September 1, 1997; 11(10): 1476 - 1485.
[Abstract] [Full Text]

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 Mol. Endocrinol.Home page
T. A. Jackson, J. K. Richer, D. L. Bain, G. S. Takimoto, L. Tung, and K. B. Horwitz
The Partial Agonist Activity of Antagonist-Occupied Steroid Receptors Is Controlled by a Novel Hinge Domain-Binding Coactivator L7/SPA and the Corepressors N-CoR or SMRT
Mol. Endocrinol., June 1, 1997; 11(6): 693 - 705.
[Abstract] [Full Text]

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 J. Biol. Chem.Home page
G. S. Takimoto, A. R. Hovland, D. M. Tasset, M. Y. Melville, L. Tung, and K. B. Horwitz
Role of Phosphorylation on DNA Binding and Transcriptional Functions of Human Progesterone Receptors
J. Biol. Chem., June 7, 1996; 271(23): 13308 - 13316.
[Abstract] [Full Text] [PDF]

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 Genes Dev.Home page
J P Lydon, F J DeMayo, C R Funk, S K Mani, A R Hughes, C A Montgomery, G Shyamala, O M Conneely, and B W O'Malley
Mice lacking progesterone receptor exhibit pleiotropic reproductive abnormalities.
Genes & Dev., September 15, 1995; 9(18): 2266 - 2278.
[Abstract] [PDF]

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 J. Biol. Chem.Home page
C. Schwerk, M. Klotzbücher, M. Sachs, V. Ulber, and L. Klein-Hitpass
Identification of a Transactivation Function in the Progesterone Receptor That Interacts with the TAF[IMAGE]110 Subunit of the TFIID Complex
J. Biol. Chem., September 8, 1995; 270(36): 21331 - 21338.
[Abstract] [Full Text] [PDF]

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 J. Biol. Chem.Home page
D. L. Bain, M. A. Franden, J. L. McManaman, G. S. Takimoto, and K. B. Horwitz
The N-terminal Region of Human Progesterone B-receptors. BIOPHYSICAL AND BIOCHEMICAL COMPARISON TO A-RECEPTORS
J. Biol. Chem., June 22, 2001; 276(26): 23825 - 23831.
[Abstract] [Full Text] [PDF]


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