Nuclear localization and DNA binding of ecdysone receptor and ultraspiracle
The Ecdysone receptor (EcR) is distributed between cytoplasm and nucleus in CHO cells. Nuclear localization is increased by the ligand Muristerone A. The most important heterodimerization partner Ultraspiracle (Usp) is localized predominantly in the nucleus. We used the diethylentriamine nitric oxid...
Gespeichert in:
| Veröffentlicht in: | Archives of insect biochemistry and physiology 2007-07, Vol.65 (3), p.125-133 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 133 |
|---|---|
| container_issue | 3 |
| container_start_page | 125 |
| container_title | Archives of insect biochemistry and physiology |
| container_volume | 65 |
| creator | Cronauer, M.V Braun, S Tremmel, C Kroncke, K.D Spindler-Barth, M |
| description | The Ecdysone receptor (EcR) is distributed between cytoplasm and nucleus in CHO cells. Nuclear localization is increased by the ligand Muristerone A. The most important heterodimerization partner Ultraspiracle (Usp) is localized predominantly in the nucleus. We used the diethylentriamine nitric oxide adduct DETA/NO, which releases NO and destroys the zinc-finger structure of nuclear receptors, to investigate whether nuclear EcR and Usp interact with DNA. If expressed separately, Usp and EcR in the absence of hormone do not interact with DNA. The hormone-induced increase in nuclear EcR is due to enhanced DNA binding. In the presence of Usp, EcR is shifted nearly quantitatively into the nucleus. Only a fraction (approximately 30%) of the heterodimer is sensitive to DETA/NO. Interaction of the heterodimer with DNA is mediated mainly by the C-domain of EcR. Deletion of the DNA-binding domain of Usp only slightly reduces nuclear localization of EcR/Usp, although the nuclear localization signal of Usp is not present anymore. The results indicate that EcR and Usp can enter the nucleus independently, but cotransport of both receptors mediated by dimerization via the ligand binding domains is possible even in the absence of hormone. |
| doi_str_mv | 10.1002/arch.20184 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_70664529</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>19713289</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4204-3e09769953a3ce233312f48c81312c4c3e81def2abd48ff590aee6d8053c41923</originalsourceid><addsrcrecordid>eNqFkE1P3DAQQC3UCraUS39AmxOHSoHxR2L7uFrKh4oWqYUicbG8zoS6zcaLnajd_nqyZEtv5TRzePM0eoS8o3BEAdixje77EQOqxA6Z0IJBXnImX5EJSK5zIUq2R96k9AMAdEnVLtmjspBABZuQz_PeNWhj1gRnG__Hdj60mW2r7GQ-zRa-rXx7n4U6Q1etU2gxi-hw1YX4BPVNF21a-WgHy1vyurZNwoPt3Cc3p5-uZ-f55dXZxWx6mTvBQOQcQctS64Jb7pBxzimrhXKKDosTjqOiFdbMLiqh6rrQYBHLSkHBnaCa8X1yOHpXMTz0mDqz9Mlh09gWQ5-MhLIUBdMvglRLypnagB9H0MWQUsTarKJf2rg2FMymsdk0Nk-NB_j91tovllj9Q7dRB4COwC_f4Po_KjP9Mjv_K83HG586_P18Y-NPU0ouC3M7PzN33-and1Rfm83HH0a-tsHY--iTufk6qDiAVJINLR8BFHCeCg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19713289</pqid></control><display><type>article</type><title>Nuclear localization and DNA binding of ecdysone receptor and ultraspiracle</title><source>MEDLINE</source><source>Wiley Online Library All Journals</source><creator>Cronauer, M.V ; Braun, S ; Tremmel, C ; Kroncke, K.D ; Spindler-Barth, M</creator><creatorcontrib>Cronauer, M.V ; Braun, S ; Tremmel, C ; Kroncke, K.D ; Spindler-Barth, M</creatorcontrib><description>The Ecdysone receptor (EcR) is distributed between cytoplasm and nucleus in CHO cells. Nuclear localization is increased by the ligand Muristerone A. The most important heterodimerization partner Ultraspiracle (Usp) is localized predominantly in the nucleus. We used the diethylentriamine nitric oxide adduct DETA/NO, which releases NO and destroys the zinc-finger structure of nuclear receptors, to investigate whether nuclear EcR and Usp interact with DNA. If expressed separately, Usp and EcR in the absence of hormone do not interact with DNA. The hormone-induced increase in nuclear EcR is due to enhanced DNA binding. In the presence of Usp, EcR is shifted nearly quantitatively into the nucleus. Only a fraction (approximately 30%) of the heterodimer is sensitive to DETA/NO. Interaction of the heterodimer with DNA is mediated mainly by the C-domain of EcR. Deletion of the DNA-binding domain of Usp only slightly reduces nuclear localization of EcR/Usp, although the nuclear localization signal of Usp is not present anymore. The results indicate that EcR and Usp can enter the nucleus independently, but cotransport of both receptors mediated by dimerization via the ligand binding domains is possible even in the absence of hormone.</description><identifier>ISSN: 0739-4462</identifier><identifier>EISSN: 1520-6327</identifier><identifier>DOI: 10.1002/arch.20184</identifier><identifier>PMID: 17570142</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>active transport ; Active Transport, Cell Nucleus ; Animals ; binding properties ; cell nucleus ; Cell Nucleus - metabolism ; CHO Cells ; Cricetinae ; Cricetulus ; dimerization ; DNA - metabolism ; DNA-binding domains ; DNA-binding proteins ; DNA-Binding Proteins - metabolism ; Drosophila melanogaster ; Drosophila Proteins ; ecdysone ; ecdysteroids ; heterodimers ; hormonal regulation ; insect ; intracellular localization ; molting hormone ; muristerone A ; nitric oxide ; nuclear receptors ; Protein Binding ; protein conformation ; Protein Structure, Tertiary ; receptors ; Receptors, Steroid - metabolism ; Transcription Factors - metabolism ; zinc finger motif ; Zn-finger</subject><ispartof>Archives of insect biochemistry and physiology, 2007-07, Vol.65 (3), p.125-133</ispartof><rights>Copyright © 2007 Wiley‐Liss, Inc.</rights><rights>(c) 2007 Wiley-Liss, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4204-3e09769953a3ce233312f48c81312c4c3e81def2abd48ff590aee6d8053c41923</citedby><cites>FETCH-LOGICAL-c4204-3e09769953a3ce233312f48c81312c4c3e81def2abd48ff590aee6d8053c41923</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Farch.20184$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Farch.20184$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17570142$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cronauer, M.V</creatorcontrib><creatorcontrib>Braun, S</creatorcontrib><creatorcontrib>Tremmel, C</creatorcontrib><creatorcontrib>Kroncke, K.D</creatorcontrib><creatorcontrib>Spindler-Barth, M</creatorcontrib><title>Nuclear localization and DNA binding of ecdysone receptor and ultraspiracle</title><title>Archives of insect biochemistry and physiology</title><addtitle>Arch. Insect Biochem. Physiol</addtitle><description>The Ecdysone receptor (EcR) is distributed between cytoplasm and nucleus in CHO cells. Nuclear localization is increased by the ligand Muristerone A. The most important heterodimerization partner Ultraspiracle (Usp) is localized predominantly in the nucleus. We used the diethylentriamine nitric oxide adduct DETA/NO, which releases NO and destroys the zinc-finger structure of nuclear receptors, to investigate whether nuclear EcR and Usp interact with DNA. If expressed separately, Usp and EcR in the absence of hormone do not interact with DNA. The hormone-induced increase in nuclear EcR is due to enhanced DNA binding. In the presence of Usp, EcR is shifted nearly quantitatively into the nucleus. Only a fraction (approximately 30%) of the heterodimer is sensitive to DETA/NO. Interaction of the heterodimer with DNA is mediated mainly by the C-domain of EcR. Deletion of the DNA-binding domain of Usp only slightly reduces nuclear localization of EcR/Usp, although the nuclear localization signal of Usp is not present anymore. The results indicate that EcR and Usp can enter the nucleus independently, but cotransport of both receptors mediated by dimerization via the ligand binding domains is possible even in the absence of hormone.</description><subject>active transport</subject><subject>Active Transport, Cell Nucleus</subject><subject>Animals</subject><subject>binding properties</subject><subject>cell nucleus</subject><subject>Cell Nucleus - metabolism</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>dimerization</subject><subject>DNA - metabolism</subject><subject>DNA-binding domains</subject><subject>DNA-binding proteins</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Drosophila melanogaster</subject><subject>Drosophila Proteins</subject><subject>ecdysone</subject><subject>ecdysteroids</subject><subject>heterodimers</subject><subject>hormonal regulation</subject><subject>insect</subject><subject>intracellular localization</subject><subject>molting hormone</subject><subject>muristerone A</subject><subject>nitric oxide</subject><subject>nuclear receptors</subject><subject>Protein Binding</subject><subject>protein conformation</subject><subject>Protein Structure, Tertiary</subject><subject>receptors</subject><subject>Receptors, Steroid - metabolism</subject><subject>Transcription Factors - metabolism</subject><subject>zinc finger motif</subject><subject>Zn-finger</subject><issn>0739-4462</issn><issn>1520-6327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1P3DAQQC3UCraUS39AmxOHSoHxR2L7uFrKh4oWqYUicbG8zoS6zcaLnajd_nqyZEtv5TRzePM0eoS8o3BEAdixje77EQOqxA6Z0IJBXnImX5EJSK5zIUq2R96k9AMAdEnVLtmjspBABZuQz_PeNWhj1gRnG__Hdj60mW2r7GQ-zRa-rXx7n4U6Q1etU2gxi-hw1YX4BPVNF21a-WgHy1vyurZNwoPt3Cc3p5-uZ-f55dXZxWx6mTvBQOQcQctS64Jb7pBxzimrhXKKDosTjqOiFdbMLiqh6rrQYBHLSkHBnaCa8X1yOHpXMTz0mDqz9Mlh09gWQ5-MhLIUBdMvglRLypnagB9H0MWQUsTarKJf2rg2FMymsdk0Nk-NB_j91tovllj9Q7dRB4COwC_f4Po_KjP9Mjv_K83HG586_P18Y-NPU0ouC3M7PzN33-and1Rfm83HH0a-tsHY--iTufk6qDiAVJINLR8BFHCeCg</recordid><startdate>200707</startdate><enddate>200707</enddate><creator>Cronauer, M.V</creator><creator>Braun, S</creator><creator>Tremmel, C</creator><creator>Kroncke, K.D</creator><creator>Spindler-Barth, M</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>FBQ</scope><scope>BSCLL</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>7SS</scope><scope>7X8</scope></search><sort><creationdate>200707</creationdate><title>Nuclear localization and DNA binding of ecdysone receptor and ultraspiracle</title><author>Cronauer, M.V ; Braun, S ; Tremmel, C ; Kroncke, K.D ; Spindler-Barth, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4204-3e09769953a3ce233312f48c81312c4c3e81def2abd48ff590aee6d8053c41923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>active transport</topic><topic>Active Transport, Cell Nucleus</topic><topic>Animals</topic><topic>binding properties</topic><topic>cell nucleus</topic><topic>Cell Nucleus - metabolism</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Cricetulus</topic><topic>dimerization</topic><topic>DNA - metabolism</topic><topic>DNA-binding domains</topic><topic>DNA-binding proteins</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Drosophila melanogaster</topic><topic>Drosophila Proteins</topic><topic>ecdysone</topic><topic>ecdysteroids</topic><topic>heterodimers</topic><topic>hormonal regulation</topic><topic>insect</topic><topic>intracellular localization</topic><topic>molting hormone</topic><topic>muristerone A</topic><topic>nitric oxide</topic><topic>nuclear receptors</topic><topic>Protein Binding</topic><topic>protein conformation</topic><topic>Protein Structure, Tertiary</topic><topic>receptors</topic><topic>Receptors, Steroid - metabolism</topic><topic>Transcription Factors - metabolism</topic><topic>zinc finger motif</topic><topic>Zn-finger</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cronauer, M.V</creatorcontrib><creatorcontrib>Braun, S</creatorcontrib><creatorcontrib>Tremmel, C</creatorcontrib><creatorcontrib>Kroncke, K.D</creatorcontrib><creatorcontrib>Spindler-Barth, M</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of insect biochemistry and physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cronauer, M.V</au><au>Braun, S</au><au>Tremmel, C</au><au>Kroncke, K.D</au><au>Spindler-Barth, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nuclear localization and DNA binding of ecdysone receptor and ultraspiracle</atitle><jtitle>Archives of insect biochemistry and physiology</jtitle><addtitle>Arch. Insect Biochem. Physiol</addtitle><date>2007-07</date><risdate>2007</risdate><volume>65</volume><issue>3</issue><spage>125</spage><epage>133</epage><pages>125-133</pages><issn>0739-4462</issn><eissn>1520-6327</eissn><abstract>The Ecdysone receptor (EcR) is distributed between cytoplasm and nucleus in CHO cells. Nuclear localization is increased by the ligand Muristerone A. The most important heterodimerization partner Ultraspiracle (Usp) is localized predominantly in the nucleus. We used the diethylentriamine nitric oxide adduct DETA/NO, which releases NO and destroys the zinc-finger structure of nuclear receptors, to investigate whether nuclear EcR and Usp interact with DNA. If expressed separately, Usp and EcR in the absence of hormone do not interact with DNA. The hormone-induced increase in nuclear EcR is due to enhanced DNA binding. In the presence of Usp, EcR is shifted nearly quantitatively into the nucleus. Only a fraction (approximately 30%) of the heterodimer is sensitive to DETA/NO. Interaction of the heterodimer with DNA is mediated mainly by the C-domain of EcR. Deletion of the DNA-binding domain of Usp only slightly reduces nuclear localization of EcR/Usp, although the nuclear localization signal of Usp is not present anymore. The results indicate that EcR and Usp can enter the nucleus independently, but cotransport of both receptors mediated by dimerization via the ligand binding domains is possible even in the absence of hormone.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>17570142</pmid><doi>10.1002/arch.20184</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0739-4462 |
| ispartof | Archives of insect biochemistry and physiology, 2007-07, Vol.65 (3), p.125-133 |
| issn | 0739-4462 1520-6327 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70664529 |
| source | MEDLINE; Wiley Online Library All Journals |
| subjects | active transport Active Transport, Cell Nucleus Animals binding properties cell nucleus Cell Nucleus - metabolism CHO Cells Cricetinae Cricetulus dimerization DNA - metabolism DNA-binding domains DNA-binding proteins DNA-Binding Proteins - metabolism Drosophila melanogaster Drosophila Proteins ecdysone ecdysteroids heterodimers hormonal regulation insect intracellular localization molting hormone muristerone A nitric oxide nuclear receptors Protein Binding protein conformation Protein Structure, Tertiary receptors Receptors, Steroid - metabolism Transcription Factors - metabolism zinc finger motif Zn-finger |
| title | Nuclear localization and DNA binding of ecdysone receptor and ultraspiracle |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T10%3A22%3A17IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Nuclear%20localization%20and%20DNA%20binding%20of%20ecdysone%20receptor%20and%20ultraspiracle&rft.jtitle=Archives%20of%20insect%20biochemistry%20and%20physiology&rft.au=Cronauer,%20M.V&rft.date=2007-07&rft.volume=65&rft.issue=3&rft.spage=125&rft.epage=133&rft.pages=125-133&rft.issn=0739-4462&rft.eissn=1520-6327&rft_id=info:doi/10.1002/arch.20184&rft_dat=%3Cproquest_cross%3E19713289%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=19713289&rft_id=info:pmid/17570142&rfr_iscdi=true |