Tumor suppressor protein p53 recruits human Sin3B/HDAC1 complex for down-regulation of its target promoters in response to genotoxic stress
Master regulator protein p53, popularly known as the "guardian of genome" is the hub for regulation of diverse cellular pathways. Depending on the cell type and severity of DNA damage, p53 protein mediates cell cycle arrest or apoptosis, besides activating DNA repair, which is apparently a...
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| Veröffentlicht in: | PloS one 2011-10, Vol.6 (10), p.e26156 |
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| creator | Bansal, Nidhi Kadamb, Rama Mittal, Shilpi Vig, Leena Sharma, Raisha Dwarakanath, Bilikere S Saluja, Daman |
| description | Master regulator protein p53, popularly known as the "guardian of genome" is the hub for regulation of diverse cellular pathways. Depending on the cell type and severity of DNA damage, p53 protein mediates cell cycle arrest or apoptosis, besides activating DNA repair, which is apparently achieved by regulation of its target genes, as well as direct interaction with other proteins. p53 is known to repress target genes via multiple mechanisms one of which is via recruitment of chromatin remodelling Sin3/HDAC1/2 complex. Sin3 proteins (Sin3A and Sin3B) regulate gene expression at the chromatin-level by serving as an anchor onto which the core Sin3/HDAC complex is assembled. The Sin3/HDAC co-repressor complex can be recruited by a large number of DNA-binding transcription factors. Sin3A has been closely linked to p53 while Sin3B is considered to be a close associate of E2Fs. The theme of this study was to establish the role of Sin3B in p53-mediated gene repression. We demonstrate a direct protein-protein interaction between human p53 and Sin3B (hSin3B). Amino acids 1-399 of hSin3B protein are involved in its interaction with N-terminal region (amino acids 1-108) of p53. Genotoxic stress induced by Adriamycin treatment increases the levels of hSin3B that is recruited to the promoters of p53-target genes (HSPA8, MAD1 and CRYZ). More importantly recruitment of hSin3B and repression of the three p53-target promoters upon Adriamycin treatment were observed only in p53(+/+) cell lines. Additionally an increased tri-methylation of the H3K9 residue at the promoters of HSPA8 and CRYZ was also observed following Adriamycin treatment. The present study highlights for the first time the essential role of Sin3B as an important associate of p53 in mediating the cellular responses to stress and in the transcriptional repression of genes encoding for heat shock proteins or proteins involved in regulation of cell cycle and apoptosis. |
| doi_str_mv | 10.1371/journal.pone.0026156 |
| format | Article |
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Depending on the cell type and severity of DNA damage, p53 protein mediates cell cycle arrest or apoptosis, besides activating DNA repair, which is apparently achieved by regulation of its target genes, as well as direct interaction with other proteins. p53 is known to repress target genes via multiple mechanisms one of which is via recruitment of chromatin remodelling Sin3/HDAC1/2 complex. Sin3 proteins (Sin3A and Sin3B) regulate gene expression at the chromatin-level by serving as an anchor onto which the core Sin3/HDAC complex is assembled. The Sin3/HDAC co-repressor complex can be recruited by a large number of DNA-binding transcription factors. Sin3A has been closely linked to p53 while Sin3B is considered to be a close associate of E2Fs. The theme of this study was to establish the role of Sin3B in p53-mediated gene repression. We demonstrate a direct protein-protein interaction between human p53 and Sin3B (hSin3B). Amino acids 1-399 of hSin3B protein are involved in its interaction with N-terminal region (amino acids 1-108) of p53. Genotoxic stress induced by Adriamycin treatment increases the levels of hSin3B that is recruited to the promoters of p53-target genes (HSPA8, MAD1 and CRYZ). More importantly recruitment of hSin3B and repression of the three p53-target promoters upon Adriamycin treatment were observed only in p53(+/+) cell lines. Additionally an increased tri-methylation of the H3K9 residue at the promoters of HSPA8 and CRYZ was also observed following Adriamycin treatment. The present study highlights for the first time the essential role of Sin3B as an important associate of p53 in mediating the cellular responses to stress and in the transcriptional repression of genes encoding for heat shock proteins or proteins involved in regulation of cell cycle and apoptosis.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0026156</identifier><identifier>PMID: 22028823</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino acids ; Animals ; Anthracyclines ; Apoptosis ; Biology ; Biomedical research ; Cell cycle ; Cell Cycle Proteins - genetics ; Cell Line, Tumor ; Cell lines ; Chromatin ; Chromatin remodeling ; Deoxyribonucleic acid ; DNA ; DNA binding proteins ; DNA Damage ; DNA methylation ; DNA repair ; Down-Regulation - drug effects ; Doxorubicin - pharmacology ; Experiments ; Gene expression ; Gene regulation ; Gene silencing ; Gene Silencing - drug effects ; Genes ; Genomes ; Genotoxicity ; Heat shock proteins ; Histone deacetylase ; Histone Deacetylase 1 - metabolism ; Histones - chemistry ; Histones - metabolism ; HSC70 Heat-Shock Proteins - genetics ; Humans ; Immunoglobulins ; Kinases ; Leukemia ; Lysine - metabolism ; Methylation ; Methylation - drug effects ; Mice ; Nuclear Proteins - genetics ; p53 Protein ; Phosphorylation ; Phosphorylation - drug effects ; Promoter Regions, Genetic - drug effects ; Promoter Regions, Genetic - genetics ; Promoters ; Protein interaction ; Protein Structure, Tertiary ; Protein-protein interactions ; Proteins ; Recruitment ; Repressor Proteins - chemistry ; Repressor Proteins - metabolism ; Stresses ; Transcription (Genetics) ; Transcription factors ; Tumor proteins ; Tumor suppressor genes ; Tumor Suppressor Protein p53 - metabolism ; Tumor suppressor proteins ; Tumors ; zeta-Crystallins - genetics</subject><ispartof>PloS one, 2011-10, Vol.6 (10), p.e26156</ispartof><rights>COPYRIGHT 2011 Public Library of Science</rights><rights>2011 Bansal et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Bansal et al. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c691t-2c8dd731e3afe4846674bb025a39e5e62aac526c2149529362103584a04ce1c3</citedby><cites>FETCH-LOGICAL-c691t-2c8dd731e3afe4846674bb025a39e5e62aac526c2149529362103584a04ce1c3</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/PMC3197607/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3197607/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2100,2926,23865,27923,27924,53790,53792,79371,79372</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22028823$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Gartel, Andrei L.</contributor><creatorcontrib>Bansal, Nidhi</creatorcontrib><creatorcontrib>Kadamb, Rama</creatorcontrib><creatorcontrib>Mittal, Shilpi</creatorcontrib><creatorcontrib>Vig, Leena</creatorcontrib><creatorcontrib>Sharma, Raisha</creatorcontrib><creatorcontrib>Dwarakanath, Bilikere S</creatorcontrib><creatorcontrib>Saluja, Daman</creatorcontrib><title>Tumor suppressor protein p53 recruits human Sin3B/HDAC1 complex for down-regulation of its target promoters in response to genotoxic stress</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Master regulator protein p53, popularly known as the "guardian of genome" is the hub for regulation of diverse cellular pathways. Depending on the cell type and severity of DNA damage, p53 protein mediates cell cycle arrest or apoptosis, besides activating DNA repair, which is apparently achieved by regulation of its target genes, as well as direct interaction with other proteins. p53 is known to repress target genes via multiple mechanisms one of which is via recruitment of chromatin remodelling Sin3/HDAC1/2 complex. Sin3 proteins (Sin3A and Sin3B) regulate gene expression at the chromatin-level by serving as an anchor onto which the core Sin3/HDAC complex is assembled. The Sin3/HDAC co-repressor complex can be recruited by a large number of DNA-binding transcription factors. Sin3A has been closely linked to p53 while Sin3B is considered to be a close associate of E2Fs. The theme of this study was to establish the role of Sin3B in p53-mediated gene repression. We demonstrate a direct protein-protein interaction between human p53 and Sin3B (hSin3B). Amino acids 1-399 of hSin3B protein are involved in its interaction with N-terminal region (amino acids 1-108) of p53. Genotoxic stress induced by Adriamycin treatment increases the levels of hSin3B that is recruited to the promoters of p53-target genes (HSPA8, MAD1 and CRYZ). More importantly recruitment of hSin3B and repression of the three p53-target promoters upon Adriamycin treatment were observed only in p53(+/+) cell lines. Additionally an increased tri-methylation of the H3K9 residue at the promoters of HSPA8 and CRYZ was also observed following Adriamycin treatment. The present study highlights for the first time the essential role of Sin3B as an important associate of p53 in mediating the cellular responses to stress and in the transcriptional repression of genes encoding for heat shock proteins or proteins involved in regulation of cell cycle and apoptosis.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Anthracyclines</subject><subject>Apoptosis</subject><subject>Biology</subject><subject>Biomedical research</subject><subject>Cell cycle</subject><subject>Cell Cycle Proteins - genetics</subject><subject>Cell Line, Tumor</subject><subject>Cell lines</subject><subject>Chromatin</subject><subject>Chromatin remodeling</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA binding proteins</subject><subject>DNA Damage</subject><subject>DNA methylation</subject><subject>DNA repair</subject><subject>Down-Regulation - drug effects</subject><subject>Doxorubicin - pharmacology</subject><subject>Experiments</subject><subject>Gene expression</subject><subject>Gene regulation</subject><subject>Gene silencing</subject><subject>Gene Silencing - 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chemistry</subject><subject>Repressor Proteins - metabolism</subject><subject>Stresses</subject><subject>Transcription (Genetics)</subject><subject>Transcription factors</subject><subject>Tumor proteins</subject><subject>Tumor suppressor genes</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><subject>Tumor suppressor proteins</subject><subject>Tumors</subject><subject>zeta-Crystallins - genetics</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNk12LEzEUhgdR3HX1H4gGBMGLdvMxyWRuhFo_trCw4BZvQ5o5M02ZmcwmGa2_wT9tartLCwqSi4ST533P4XBOlr0keEpYQS43bvS9bqeD62GKMRWEi0fZOSkZnQiK2eOj91n2LIQNxpxJIZ5mZ5RiKiVl59mv5dg5j8I4DB5CSM_Buwi2RwNnyIPxo40BrcdO9-jW9uzD5dXH2Zwg47qhhS2qk6RyP_qJh2ZsdbSuR65GO1HUvoG4M-ySpQ8ouaYkqeAAKDrUQO-i21qDQtwlf549qXUb4MXhvsiWnz8t51eT65svi_nsemJESeKEGllVBSPAdA25zIUo8tUKU65ZCRwE1dpwKgwleclpyQQlmHGZa5wbIIZdZK_3tkPrgjq0MSjCCKYFlVQkYrEnKqc3avC20_6nctqqPwHnG6V9tKYFxbWWoKWpqormWkApgYtVzYUEyiWvk9f7Q7Zx1UFloI9etyempz-9XavGfVeMlIXARTJ4czDw7m6EEP9R8oFqdKrK9rVLZqazwahZXggpCsZpoqZ_odKpoLMmDVJtU_xE8O5EkJgI29joMQS1uP36_-zNt1P27RG7Bt3GdXDtuBufcArme9B4F4KH-qFzBKvdHtx3Q-32QB32IMleHXf9QXQ_-Ow3sI0E4w</recordid><startdate>20111020</startdate><enddate>20111020</enddate><creator>Bansal, Nidhi</creator><creator>Kadamb, Rama</creator><creator>Mittal, Shilpi</creator><creator>Vig, Leena</creator><creator>Sharma, Raisha</creator><creator>Dwarakanath, Bilikere S</creator><creator>Saluja, Daman</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20111020</creationdate><title>Tumor suppressor protein p53 recruits human Sin3B/HDAC1 complex for down-regulation of its target promoters in response to genotoxic stress</title><author>Bansal, Nidhi ; Kadamb, Rama ; Mittal, Shilpi ; Vig, Leena ; Sharma, Raisha ; Dwarakanath, Bilikere S ; Saluja, Daman</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c691t-2c8dd731e3afe4846674bb025a39e5e62aac526c2149529362103584a04ce1c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino acids</topic><topic>Animals</topic><topic>Anthracyclines</topic><topic>Apoptosis</topic><topic>Biology</topic><topic>Biomedical research</topic><topic>Cell cycle</topic><topic>Cell Cycle Proteins - genetics</topic><topic>Cell Line, Tumor</topic><topic>Cell lines</topic><topic>Chromatin</topic><topic>Chromatin remodeling</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA binding proteins</topic><topic>DNA Damage</topic><topic>DNA methylation</topic><topic>DNA repair</topic><topic>Down-Regulation - drug effects</topic><topic>Doxorubicin - pharmacology</topic><topic>Experiments</topic><topic>Gene expression</topic><topic>Gene regulation</topic><topic>Gene silencing</topic><topic>Gene Silencing - drug effects</topic><topic>Genes</topic><topic>Genomes</topic><topic>Genotoxicity</topic><topic>Heat shock proteins</topic><topic>Histone deacetylase</topic><topic>Histone Deacetylase 1 - metabolism</topic><topic>Histones - chemistry</topic><topic>Histones - metabolism</topic><topic>HSC70 Heat-Shock Proteins - genetics</topic><topic>Humans</topic><topic>Immunoglobulins</topic><topic>Kinases</topic><topic>Leukemia</topic><topic>Lysine - metabolism</topic><topic>Methylation</topic><topic>Methylation - drug effects</topic><topic>Mice</topic><topic>Nuclear Proteins - genetics</topic><topic>p53 Protein</topic><topic>Phosphorylation</topic><topic>Phosphorylation - drug effects</topic><topic>Promoter Regions, Genetic - drug effects</topic><topic>Promoter Regions, Genetic - genetics</topic><topic>Promoters</topic><topic>Protein interaction</topic><topic>Protein Structure, Tertiary</topic><topic>Protein-protein interactions</topic><topic>Proteins</topic><topic>Recruitment</topic><topic>Repressor Proteins - chemistry</topic><topic>Repressor Proteins - metabolism</topic><topic>Stresses</topic><topic>Transcription (Genetics)</topic><topic>Transcription factors</topic><topic>Tumor proteins</topic><topic>Tumor suppressor genes</topic><topic>Tumor Suppressor Protein p53 - metabolism</topic><topic>Tumor suppressor proteins</topic><topic>Tumors</topic><topic>zeta-Crystallins - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bansal, Nidhi</creatorcontrib><creatorcontrib>Kadamb, Rama</creatorcontrib><creatorcontrib>Mittal, Shilpi</creatorcontrib><creatorcontrib>Vig, Leena</creatorcontrib><creatorcontrib>Sharma, Raisha</creatorcontrib><creatorcontrib>Dwarakanath, Bilikere S</creatorcontrib><creatorcontrib>Saluja, Daman</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</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 Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content 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 China</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bansal, Nidhi</au><au>Kadamb, Rama</au><au>Mittal, Shilpi</au><au>Vig, Leena</au><au>Sharma, Raisha</au><au>Dwarakanath, Bilikere S</au><au>Saluja, Daman</au><au>Gartel, Andrei L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tumor suppressor protein p53 recruits human Sin3B/HDAC1 complex for down-regulation of its target promoters in response to genotoxic stress</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2011-10-20</date><risdate>2011</risdate><volume>6</volume><issue>10</issue><spage>e26156</spage><pages>e26156-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Master regulator protein p53, popularly known as the "guardian of genome" is the hub for regulation of diverse cellular pathways. Depending on the cell type and severity of DNA damage, p53 protein mediates cell cycle arrest or apoptosis, besides activating DNA repair, which is apparently achieved by regulation of its target genes, as well as direct interaction with other proteins. p53 is known to repress target genes via multiple mechanisms one of which is via recruitment of chromatin remodelling Sin3/HDAC1/2 complex. Sin3 proteins (Sin3A and Sin3B) regulate gene expression at the chromatin-level by serving as an anchor onto which the core Sin3/HDAC complex is assembled. The Sin3/HDAC co-repressor complex can be recruited by a large number of DNA-binding transcription factors. Sin3A has been closely linked to p53 while Sin3B is considered to be a close associate of E2Fs. The theme of this study was to establish the role of Sin3B in p53-mediated gene repression. We demonstrate a direct protein-protein interaction between human p53 and Sin3B (hSin3B). Amino acids 1-399 of hSin3B protein are involved in its interaction with N-terminal region (amino acids 1-108) of p53. Genotoxic stress induced by Adriamycin treatment increases the levels of hSin3B that is recruited to the promoters of p53-target genes (HSPA8, MAD1 and CRYZ). More importantly recruitment of hSin3B and repression of the three p53-target promoters upon Adriamycin treatment were observed only in p53(+/+) cell lines. Additionally an increased tri-methylation of the H3K9 residue at the promoters of HSPA8 and CRYZ was also observed following Adriamycin treatment. The present study highlights for the first time the essential role of Sin3B as an important associate of p53 in mediating the cellular responses to stress and in the transcriptional repression of genes encoding for heat shock proteins or proteins involved in regulation of cell cycle and apoptosis.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22028823</pmid><doi>10.1371/journal.pone.0026156</doi><tpages>e26156</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2011-10, Vol.6 (10), p.e26156 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1310272826 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS); EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino acids Animals Anthracyclines Apoptosis Biology Biomedical research Cell cycle Cell Cycle Proteins - genetics Cell Line, Tumor Cell lines Chromatin Chromatin remodeling Deoxyribonucleic acid DNA DNA binding proteins DNA Damage DNA methylation DNA repair Down-Regulation - drug effects Doxorubicin - pharmacology Experiments Gene expression Gene regulation Gene silencing Gene Silencing - drug effects Genes Genomes Genotoxicity Heat shock proteins Histone deacetylase Histone Deacetylase 1 - metabolism Histones - chemistry Histones - metabolism HSC70 Heat-Shock Proteins - genetics Humans Immunoglobulins Kinases Leukemia Lysine - metabolism Methylation Methylation - drug effects Mice Nuclear Proteins - genetics p53 Protein Phosphorylation Phosphorylation - drug effects Promoter Regions, Genetic - drug effects Promoter Regions, Genetic - genetics Promoters Protein interaction Protein Structure, Tertiary Protein-protein interactions Proteins Recruitment Repressor Proteins - chemistry Repressor Proteins - metabolism Stresses Transcription (Genetics) Transcription factors Tumor proteins Tumor suppressor genes Tumor Suppressor Protein p53 - metabolism Tumor suppressor proteins Tumors zeta-Crystallins - genetics |
| title | Tumor suppressor protein p53 recruits human Sin3B/HDAC1 complex for down-regulation of its target promoters in response to genotoxic stress |
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