Regulation of matrix attachment region-dependent, lymphocyte-restricted transcription through differential localization within promyelocytic leukemia nuclear bodies
Bright ( B cell r egulator of IgH t ranscription) transactivates the immunoglobulin heavy chain (IgH) intronic enhancer, Eμ, by binding to matrix attachment regions (MARs), sites necessary for DNA attachment to the nuclear matrix. Here we report that Bright interacts with the ubiquitous autoantigen...
Gespeichert in:
| Veröffentlicht in: | The EMBO journal 2000-08, Vol.19 (15), p.4123-4133 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 4133 |
|---|---|
| container_issue | 15 |
| container_start_page | 4123 |
| container_title | The EMBO journal |
| container_volume | 19 |
| creator | Zong, Rui-Ting Das, Chhaya Tucker, Philip W. |
| description | Bright (
B
cell
r
egulator of
IgH
t
ranscription) transactivates the immunoglobulin heavy chain (IgH) intronic enhancer, Eμ, by binding to matrix attachment regions (MARs), sites necessary for DNA attachment to the nuclear matrix. Here we report that Bright interacts with the ubiquitous autoantigen Sp100, a component of promyelocytic leukemia nuclear bodies (PML NBs), and with LYSp100B/Sp140, the lymphoid‐restricted homolog of Sp100. Both in intact cells and in nuclear matrix preparations, the majority of Bright and Sp100 colocalize within PML NBs. In contrast, Bright colocalizes with only a small fraction of LYSp100B while inducing a redistribution of the majority of LYSp100B from its associated nuclear domains (LANDs) into nucleoplasm and cytoplasm. Sp100 represses the MAR‐binding and transactivation activity of Bright. LYSp100B interacts more weakly with Bright but requires significantly higher levels than Sp100 to inhibit MAR binding. However, it strongly stimulates Bright transactivation through Eμ. We suggest that Sp100 and LYSp100B interactions with Bright have different consequences for IgH transcription, potentially through differential association of Eμ MARs with nuclear matrix‐ associated PML NBs and LANDs. |
| doi_str_mv | 10.1093/emboj/19.15.4123 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_306587</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71269212</sourcerecordid><originalsourceid>FETCH-LOGICAL-c6678-6822b9c46b4b9b2487c468ba8eb6a08d5d5cc6748a57f400b0baf031a426aef3</originalsourceid><addsrcrecordid>eNqFkk9v1DAQxSMEokvhzgVkceBEtv6T2MmhB6hKC5QioUocLceZbNw6cbAT2uXz8EHxNtWyIKGebPm935vxaJLkOcFLgkt2AF3lLg9IuST5MiOUPUgWJOM4pVjkD5MFppykGSnKveRJCJcY47wQ5HGyF2Ean-ki-fUVVpNVo3E9cg3q1OjNDVLjqHTbQT8iD6uopTUM0Nfx4Q2y625onV6PkHoI0a9HqNHoVR-0N8Nt1Nh6N61aVJumAR8xoyyyTitrfs7Frs3Ymh4N3nVrsJs4o5GF6Qo6o1A_aQvKo8rVBsLT5FGjbIBnd-d-cvH--OLoND37cvLh6O1ZqjkXRcoLSqtSZ7zKqrKiWSHivahUARVXuKjzOteai6xQuWgyjCtcqQYzojLKFTRsPzmcY4ep6qDWsW2vrBy86ZRfS6eM_FvpTStX7odkmMfBRv71He_d9ymORnYmaLBW9eCmIAWhPM6d3mskgjMhOI_GV_8YL93k-zgDScqcckzFpiyeTdq7EDw0244Jlps1kbdrEglJcrlZk4i83P3pDjDvRTSUs-HaWFjfGyiPP7_7KPKSUVpElsxsiFi_Ar_T9P8bejEzvRonD9uCfzLTWTdhhJutrPyV5IKJXH47P5Gn558YZoxKxn4D54z7Yg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>195260277</pqid></control><display><type>article</type><title>Regulation of matrix attachment region-dependent, lymphocyte-restricted transcription through differential localization within promyelocytic leukemia nuclear bodies</title><source>MEDLINE</source><source>Wiley Free Content</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Wiley Online Library All Journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Zong, Rui-Ting ; Das, Chhaya ; Tucker, Philip W.</creator><creatorcontrib>Zong, Rui-Ting ; Das, Chhaya ; Tucker, Philip W.</creatorcontrib><description>Bright (
B
cell
r
egulator of
IgH
t
ranscription) transactivates the immunoglobulin heavy chain (IgH) intronic enhancer, Eμ, by binding to matrix attachment regions (MARs), sites necessary for DNA attachment to the nuclear matrix. Here we report that Bright interacts with the ubiquitous autoantigen Sp100, a component of promyelocytic leukemia nuclear bodies (PML NBs), and with LYSp100B/Sp140, the lymphoid‐restricted homolog of Sp100. Both in intact cells and in nuclear matrix preparations, the majority of Bright and Sp100 colocalize within PML NBs. In contrast, Bright colocalizes with only a small fraction of LYSp100B while inducing a redistribution of the majority of LYSp100B from its associated nuclear domains (LANDs) into nucleoplasm and cytoplasm. Sp100 represses the MAR‐binding and transactivation activity of Bright. LYSp100B interacts more weakly with Bright but requires significantly higher levels than Sp100 to inhibit MAR binding. However, it strongly stimulates Bright transactivation through Eμ. We suggest that Sp100 and LYSp100B interactions with Bright have different consequences for IgH transcription, potentially through differential association of Eμ MARs with nuclear matrix‐ associated PML NBs and LANDs.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/19.15.4123</identifier><identifier>PMID: 10921892</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Antigens, Nuclear ; autoantigen ; Autoantigens - metabolism ; Cell Compartmentation ; Cell Nucleus - ultrastructure ; DNA-Binding Proteins - metabolism ; Fluorescent Antibody Technique ; Humans ; Immunoglobulin Heavy Chains - genetics ; Leukemia ; Leukemia, Promyelocytic, Acute ; Lymphocytes ; Molecular Sequence Data ; Nuclear Matrix ; nuclear matrix attachment ; Nuclear Proteins - metabolism ; Oncogenes ; PML nuclear bodies ; Protein Binding ; Sp100 proten ; Trans-Activators - metabolism ; Transcription Factors ; transcription regulation ; Transcriptional Activation ; Tumor Cells, Cultured ; Two-Hybrid System Techniques</subject><ispartof>The EMBO journal, 2000-08, Vol.19 (15), p.4123-4133</ispartof><rights>European Molecular Biology Organization 2000</rights><rights>Copyright © 2000 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Aug 01, 2000</rights><rights>Copyright © 2000 European Molecular Biology Organization 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6678-6822b9c46b4b9b2487c468ba8eb6a08d5d5cc6748a57f400b0baf031a426aef3</citedby><cites>FETCH-LOGICAL-c6678-6822b9c46b4b9b2487c468ba8eb6a08d5d5cc6748a57f400b0baf031a426aef3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC306587/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC306587/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1416,1432,27923,27924,45573,45574,46408,46832,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10921892$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zong, Rui-Ting</creatorcontrib><creatorcontrib>Das, Chhaya</creatorcontrib><creatorcontrib>Tucker, Philip W.</creatorcontrib><title>Regulation of matrix attachment region-dependent, lymphocyte-restricted transcription through differential localization within promyelocytic leukemia nuclear bodies</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Bright (
B
cell
r
egulator of
IgH
t
ranscription) transactivates the immunoglobulin heavy chain (IgH) intronic enhancer, Eμ, by binding to matrix attachment regions (MARs), sites necessary for DNA attachment to the nuclear matrix. Here we report that Bright interacts with the ubiquitous autoantigen Sp100, a component of promyelocytic leukemia nuclear bodies (PML NBs), and with LYSp100B/Sp140, the lymphoid‐restricted homolog of Sp100. Both in intact cells and in nuclear matrix preparations, the majority of Bright and Sp100 colocalize within PML NBs. In contrast, Bright colocalizes with only a small fraction of LYSp100B while inducing a redistribution of the majority of LYSp100B from its associated nuclear domains (LANDs) into nucleoplasm and cytoplasm. Sp100 represses the MAR‐binding and transactivation activity of Bright. LYSp100B interacts more weakly with Bright but requires significantly higher levels than Sp100 to inhibit MAR binding. However, it strongly stimulates Bright transactivation through Eμ. We suggest that Sp100 and LYSp100B interactions with Bright have different consequences for IgH transcription, potentially through differential association of Eμ MARs with nuclear matrix‐ associated PML NBs and LANDs.</description><subject>Antigens, Nuclear</subject><subject>autoantigen</subject><subject>Autoantigens - metabolism</subject><subject>Cell Compartmentation</subject><subject>Cell Nucleus - ultrastructure</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fluorescent Antibody Technique</subject><subject>Humans</subject><subject>Immunoglobulin Heavy Chains - genetics</subject><subject>Leukemia</subject><subject>Leukemia, Promyelocytic, Acute</subject><subject>Lymphocytes</subject><subject>Molecular Sequence Data</subject><subject>Nuclear Matrix</subject><subject>nuclear matrix attachment</subject><subject>Nuclear Proteins - metabolism</subject><subject>Oncogenes</subject><subject>PML nuclear bodies</subject><subject>Protein Binding</subject><subject>Sp100 proten</subject><subject>Trans-Activators - metabolism</subject><subject>Transcription Factors</subject><subject>transcription regulation</subject><subject>Transcriptional Activation</subject><subject>Tumor Cells, Cultured</subject><subject>Two-Hybrid System Techniques</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkk9v1DAQxSMEokvhzgVkceBEtv6T2MmhB6hKC5QioUocLceZbNw6cbAT2uXz8EHxNtWyIKGebPm935vxaJLkOcFLgkt2AF3lLg9IuST5MiOUPUgWJOM4pVjkD5MFppykGSnKveRJCJcY47wQ5HGyF2Ean-ki-fUVVpNVo3E9cg3q1OjNDVLjqHTbQT8iD6uopTUM0Nfx4Q2y625onV6PkHoI0a9HqNHoVR-0N8Nt1Nh6N61aVJumAR8xoyyyTitrfs7Frs3Ymh4N3nVrsJs4o5GF6Qo6o1A_aQvKo8rVBsLT5FGjbIBnd-d-cvH--OLoND37cvLh6O1ZqjkXRcoLSqtSZ7zKqrKiWSHivahUARVXuKjzOteai6xQuWgyjCtcqQYzojLKFTRsPzmcY4ep6qDWsW2vrBy86ZRfS6eM_FvpTStX7odkmMfBRv71He_d9ymORnYmaLBW9eCmIAWhPM6d3mskgjMhOI_GV_8YL93k-zgDScqcckzFpiyeTdq7EDw0244Jlps1kbdrEglJcrlZk4i83P3pDjDvRTSUs-HaWFjfGyiPP7_7KPKSUVpElsxsiFi_Ar_T9P8bejEzvRonD9uCfzLTWTdhhJutrPyV5IKJXH47P5Gn558YZoxKxn4D54z7Yg</recordid><startdate>20000801</startdate><enddate>20000801</enddate><creator>Zong, Rui-Ting</creator><creator>Das, Chhaya</creator><creator>Tucker, Philip W.</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000801</creationdate><title>Regulation of matrix attachment region-dependent, lymphocyte-restricted transcription through differential localization within promyelocytic leukemia nuclear bodies</title><author>Zong, Rui-Ting ; Das, Chhaya ; Tucker, Philip W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6678-6822b9c46b4b9b2487c468ba8eb6a08d5d5cc6748a57f400b0baf031a426aef3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Antigens, Nuclear</topic><topic>autoantigen</topic><topic>Autoantigens - metabolism</topic><topic>Cell Compartmentation</topic><topic>Cell Nucleus - ultrastructure</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Fluorescent Antibody Technique</topic><topic>Humans</topic><topic>Immunoglobulin Heavy Chains - genetics</topic><topic>Leukemia</topic><topic>Leukemia, Promyelocytic, Acute</topic><topic>Lymphocytes</topic><topic>Molecular Sequence Data</topic><topic>Nuclear Matrix</topic><topic>nuclear matrix attachment</topic><topic>Nuclear Proteins - metabolism</topic><topic>Oncogenes</topic><topic>PML nuclear bodies</topic><topic>Protein Binding</topic><topic>Sp100 proten</topic><topic>Trans-Activators - metabolism</topic><topic>Transcription Factors</topic><topic>transcription regulation</topic><topic>Transcriptional Activation</topic><topic>Tumor Cells, Cultured</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zong, Rui-Ting</creatorcontrib><creatorcontrib>Das, Chhaya</creatorcontrib><creatorcontrib>Tucker, Philip W.</creatorcontrib><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>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zong, Rui-Ting</au><au>Das, Chhaya</au><au>Tucker, Philip W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of matrix attachment region-dependent, lymphocyte-restricted transcription through differential localization within promyelocytic leukemia nuclear bodies</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2000-08-01</date><risdate>2000</risdate><volume>19</volume><issue>15</issue><spage>4123</spage><epage>4133</epage><pages>4123-4133</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Bright (
B
cell
r
egulator of
IgH
t
ranscription) transactivates the immunoglobulin heavy chain (IgH) intronic enhancer, Eμ, by binding to matrix attachment regions (MARs), sites necessary for DNA attachment to the nuclear matrix. Here we report that Bright interacts with the ubiquitous autoantigen Sp100, a component of promyelocytic leukemia nuclear bodies (PML NBs), and with LYSp100B/Sp140, the lymphoid‐restricted homolog of Sp100. Both in intact cells and in nuclear matrix preparations, the majority of Bright and Sp100 colocalize within PML NBs. In contrast, Bright colocalizes with only a small fraction of LYSp100B while inducing a redistribution of the majority of LYSp100B from its associated nuclear domains (LANDs) into nucleoplasm and cytoplasm. Sp100 represses the MAR‐binding and transactivation activity of Bright. LYSp100B interacts more weakly with Bright but requires significantly higher levels than Sp100 to inhibit MAR binding. However, it strongly stimulates Bright transactivation through Eμ. We suggest that Sp100 and LYSp100B interactions with Bright have different consequences for IgH transcription, potentially through differential association of Eμ MARs with nuclear matrix‐ associated PML NBs and LANDs.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>10921892</pmid><doi>10.1093/emboj/19.15.4123</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0261-4189 |
| ispartof | The EMBO journal, 2000-08, Vol.19 (15), p.4123-4133 |
| issn | 0261-4189 1460-2075 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_306587 |
| source | MEDLINE; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Antigens, Nuclear autoantigen Autoantigens - metabolism Cell Compartmentation Cell Nucleus - ultrastructure DNA-Binding Proteins - metabolism Fluorescent Antibody Technique Humans Immunoglobulin Heavy Chains - genetics Leukemia Leukemia, Promyelocytic, Acute Lymphocytes Molecular Sequence Data Nuclear Matrix nuclear matrix attachment Nuclear Proteins - metabolism Oncogenes PML nuclear bodies Protein Binding Sp100 proten Trans-Activators - metabolism Transcription Factors transcription regulation Transcriptional Activation Tumor Cells, Cultured Two-Hybrid System Techniques |
| title | Regulation of matrix attachment region-dependent, lymphocyte-restricted transcription through differential localization within promyelocytic leukemia nuclear bodies |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-11T13%3A17%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Regulation%20of%20matrix%20attachment%20region-dependent,%20lymphocyte-restricted%20transcription%20through%20differential%20localization%20within%20promyelocytic%20leukemia%20nuclear%20bodies&rft.jtitle=The%20EMBO%20journal&rft.au=Zong,%20Rui-Ting&rft.date=2000-08-01&rft.volume=19&rft.issue=15&rft.spage=4123&rft.epage=4133&rft.pages=4123-4133&rft.issn=0261-4189&rft.eissn=1460-2075&rft.coden=EMJODG&rft_id=info:doi/10.1093/emboj/19.15.4123&rft_dat=%3Cproquest_pubme%3E71269212%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=195260277&rft_id=info:pmid/10921892&rfr_iscdi=true |