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An N-terminal Inhibitory Function, IF, Suppresses Transcription by the A-isoform but Not the B-isoform of Human Progesterone Receptors
The B-isoform of human progesterone receptors (PR) contains three activation functions (AF3, AF1, and AF2), two of which (AF1 and AF2) are shared with the A-isoform. AF3 is in the B-upstream segment (BUS), the far N-terminal 164 amino acids of B-receptors; AF1 is in the 392-amino acid N-terminal reg...
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| Published in: | The Journal of biological chemistry 1998-03, Vol.273 (10), p.5455-5460 |
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| Main Authors: | , , , , |
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| container_end_page | 5460 |
| container_issue | 10 |
| container_start_page | 5455 |
| container_title | The Journal of biological chemistry |
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| creator | Hovland, Alicia Rudie Powell, Roger L. Takimoto, Glenn S. Tung, Lin Horwitz, Kathryn B. |
| description | The B-isoform of human progesterone receptors (PR) contains three activation functions (AF3, AF1, and AF2), two of which (AF1 and AF2) are shared with the A-isoform. AF3 is in the B-upstream segment (BUS), the far N-terminal 164 amino acids of B-receptors; AF1 is in the 392-amino acid N-terminal region common to both receptors; and AF2 is in the C-terminal hormone binding domain. B-receptors are usually stronger transactivators than A-receptors due to transcriptional synergism between AF3 and one of the two downstream AFs. We now show that the N terminus of PR common to both isoforms contains an inhibitory function (IF) located in a 292-amino acid segment lying upstream of AF1. IF represses the activity of A-receptors but is not inhibitory in the context of B-receptors due to constraints imparted by BUS. As a result, IF inhibits AF1 or AF2 but not AF3, regardless of the position of IF relative to BUS. IF is functionally independent and strongly represses transcription when it is fused upstream of estrogen receptors. These data demonstrate the existence of a novel, transferable inhibitory function, mapping to the PR N terminus, which begins to assign specific roles to this large undefined region. |
| doi_str_mv | 10.1074/jbc.273.10.5455 |
| format | article |
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AF3 is in the B-upstream segment (BUS), the far N-terminal 164 amino acids of B-receptors; AF1 is in the 392-amino acid N-terminal region common to both receptors; and AF2 is in the C-terminal hormone binding domain. B-receptors are usually stronger transactivators than A-receptors due to transcriptional synergism between AF3 and one of the two downstream AFs. We now show that the N terminus of PR common to both isoforms contains an inhibitory function (IF) located in a 292-amino acid segment lying upstream of AF1. IF represses the activity of A-receptors but is not inhibitory in the context of B-receptors due to constraints imparted by BUS. As a result, IF inhibits AF1 or AF2 but not AF3, regardless of the position of IF relative to BUS. IF is functionally independent and strongly represses transcription when it is fused upstream of estrogen receptors. These data demonstrate the existence of a novel, transferable inhibitory function, mapping to the PR N terminus, which begins to assign specific roles to this large undefined region.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.273.10.5455</identifier><identifier>PMID: 9488667</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Gene Expression Regulation - genetics ; HeLa Cells ; Humans ; Peptide Fragments - genetics ; Peptide Fragments - pharmacology ; Receptors, Estrogen - chemistry ; Receptors, Estrogen - physiology ; Receptors, Progesterone - chemistry ; Receptors, Progesterone - physiology ; Suppression, Genetic - physiology ; Trans-Activators - chemistry ; Trans-Activators - pharmacology ; Transcription, Genetic - genetics ; Transfection - genetics</subject><ispartof>The Journal of biological chemistry, 1998-03, Vol.273 (10), p.5455-5460</ispartof><rights>1998 © 1998 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c442t-6f06baa6108afc70053d34fccc19cffa7f810bd47545b3f4168a9462179b8d7e3</citedby><cites>FETCH-LOGICAL-c442t-6f06baa6108afc70053d34fccc19cffa7f810bd47545b3f4168a9462179b8d7e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9488667$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hovland, Alicia Rudie</creatorcontrib><creatorcontrib>Powell, Roger L.</creatorcontrib><creatorcontrib>Takimoto, Glenn S.</creatorcontrib><creatorcontrib>Tung, Lin</creatorcontrib><creatorcontrib>Horwitz, Kathryn B.</creatorcontrib><title>An N-terminal Inhibitory Function, IF, Suppresses Transcription by the A-isoform but Not the B-isoform of Human Progesterone Receptors</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The B-isoform of human progesterone receptors (PR) contains three activation functions (AF3, AF1, and AF2), two of which (AF1 and AF2) are shared with the A-isoform. AF3 is in the B-upstream segment (BUS), the far N-terminal 164 amino acids of B-receptors; AF1 is in the 392-amino acid N-terminal region common to both receptors; and AF2 is in the C-terminal hormone binding domain. B-receptors are usually stronger transactivators than A-receptors due to transcriptional synergism between AF3 and one of the two downstream AFs. We now show that the N terminus of PR common to both isoforms contains an inhibitory function (IF) located in a 292-amino acid segment lying upstream of AF1. IF represses the activity of A-receptors but is not inhibitory in the context of B-receptors due to constraints imparted by BUS. As a result, IF inhibits AF1 or AF2 but not AF3, regardless of the position of IF relative to BUS. IF is functionally independent and strongly represses transcription when it is fused upstream of estrogen receptors. These data demonstrate the existence of a novel, transferable inhibitory function, mapping to the PR N terminus, which begins to assign specific roles to this large undefined region.</description><subject>Gene Expression Regulation - genetics</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Peptide Fragments - genetics</subject><subject>Peptide Fragments - pharmacology</subject><subject>Receptors, Estrogen - chemistry</subject><subject>Receptors, Estrogen - physiology</subject><subject>Receptors, Progesterone - chemistry</subject><subject>Receptors, Progesterone - physiology</subject><subject>Suppression, Genetic - physiology</subject><subject>Trans-Activators - chemistry</subject><subject>Trans-Activators - pharmacology</subject><subject>Transcription, Genetic - genetics</subject><subject>Transfection - genetics</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNp1kMFu1DAQhi1EVZbCmROSJaSemq2dOLFzXCqWrlQVBEXiZtnOuHG1sYOdFO0L8Nx4u6sekPDFmpl__pn5EHpHyZISzi4ftFmWvMrBsmZ1_QItKBFVUdX050u0IKSkRVvW4hV6ndIDyY-19BSdtkyIpuEL9Gfl8W0xQRycV1u88b3Tbgpxh9ezN5ML_gJv1hf4-zyOEVKChO-i8slEN-6rWO_w1ANeFS4FG-KA9Tzh2zA9ZT8-Z4PF1_OgPP4awz2kPDB4wN_AwJinpTfoxKptgrfH_wz9WH-6u7oubr583lytbgrDWDkVjSWNVqrJNyprOCF11VXMGmNoa6xV3ApKdMd4ZqEry2gjVMuakvJWi45DdYbOD75jDL_mvIccXDKw3SoPYU6SNqVgreBZeHkQmhhSimDlGN2g4k5SIvfkZSYvM_l9vCefO94frWc9QPesP6LO9Q-Heu_u-98ugtQumB6Gf1zagwoyhUcHUSbjwBvocoeZZBfcfzf4C0sRn14</recordid><startdate>19980306</startdate><enddate>19980306</enddate><creator>Hovland, Alicia Rudie</creator><creator>Powell, Roger L.</creator><creator>Takimoto, Glenn S.</creator><creator>Tung, Lin</creator><creator>Horwitz, Kathryn B.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope></search><sort><creationdate>19980306</creationdate><title>An N-terminal Inhibitory Function, IF, Suppresses Transcription by the A-isoform but Not the B-isoform of Human Progesterone Receptors</title><author>Hovland, Alicia Rudie ; Powell, Roger L. ; Takimoto, Glenn S. ; Tung, Lin ; Horwitz, Kathryn B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c442t-6f06baa6108afc70053d34fccc19cffa7f810bd47545b3f4168a9462179b8d7e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Gene Expression Regulation - genetics</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Peptide Fragments - genetics</topic><topic>Peptide Fragments - pharmacology</topic><topic>Receptors, Estrogen - chemistry</topic><topic>Receptors, Estrogen - physiology</topic><topic>Receptors, Progesterone - chemistry</topic><topic>Receptors, Progesterone - physiology</topic><topic>Suppression, Genetic - physiology</topic><topic>Trans-Activators - chemistry</topic><topic>Trans-Activators - pharmacology</topic><topic>Transcription, Genetic - genetics</topic><topic>Transfection - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hovland, Alicia Rudie</creatorcontrib><creatorcontrib>Powell, Roger L.</creatorcontrib><creatorcontrib>Takimoto, Glenn S.</creatorcontrib><creatorcontrib>Tung, Lin</creatorcontrib><creatorcontrib>Horwitz, Kathryn B.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hovland, Alicia Rudie</au><au>Powell, Roger L.</au><au>Takimoto, Glenn S.</au><au>Tung, Lin</au><au>Horwitz, Kathryn B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An N-terminal Inhibitory Function, IF, Suppresses Transcription by the A-isoform but Not the B-isoform of Human Progesterone Receptors</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1998-03-06</date><risdate>1998</risdate><volume>273</volume><issue>10</issue><spage>5455</spage><epage>5460</epage><pages>5455-5460</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-1</notes><notes>content type line 23</notes><abstract>The B-isoform of human progesterone receptors (PR) contains three activation functions (AF3, AF1, and AF2), two of which (AF1 and AF2) are shared with the A-isoform. AF3 is in the B-upstream segment (BUS), the far N-terminal 164 amino acids of B-receptors; AF1 is in the 392-amino acid N-terminal region common to both receptors; and AF2 is in the C-terminal hormone binding domain. B-receptors are usually stronger transactivators than A-receptors due to transcriptional synergism between AF3 and one of the two downstream AFs. We now show that the N terminus of PR common to both isoforms contains an inhibitory function (IF) located in a 292-amino acid segment lying upstream of AF1. IF represses the activity of A-receptors but is not inhibitory in the context of B-receptors due to constraints imparted by BUS. As a result, IF inhibits AF1 or AF2 but not AF3, regardless of the position of IF relative to BUS. IF is functionally independent and strongly represses transcription when it is fused upstream of estrogen receptors. These data demonstrate the existence of a novel, transferable inhibitory function, mapping to the PR N terminus, which begins to assign specific roles to this large undefined region.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9488667</pmid><doi>10.1074/jbc.273.10.5455</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1998-03, Vol.273 (10), p.5455-5460 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16284987 |
| source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS |
| subjects | Gene Expression Regulation - genetics HeLa Cells Humans Peptide Fragments - genetics Peptide Fragments - pharmacology Receptors, Estrogen - chemistry Receptors, Estrogen - physiology Receptors, Progesterone - chemistry Receptors, Progesterone - physiology Suppression, Genetic - physiology Trans-Activators - chemistry Trans-Activators - pharmacology Transcription, Genetic - genetics Transfection - genetics |
| title | An N-terminal Inhibitory Function, IF, Suppresses Transcription by the A-isoform but Not the B-isoform of Human Progesterone Receptors |
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