S/MAR-binding properties of Sox2 and its involvement in apoptosis of human NT2 neural precursors
DNA fragmentation in apoptosis, especially in lymphocytic cells, is initiated at scaffold/matrix attachment regions (S/MARs) and is preceded by the degradation of nuclear proteins. The present study was performed to establish whether the same mechanism occurred in human NT2 cells subjected to oxygen...
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| Veröffentlicht in: | Cell death and differentiation 2005-11, Vol.12 (11), p.1368-1377 |
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| creator | Lei, J X Liu, Q Y Sodja, C LeBlanc, J Ribecco-Lutkiewicz, M Smith, B Charlebois, C Walker, P R Sikorska, M |
| description | DNA fragmentation in apoptosis, especially in lymphocytic cells, is initiated at scaffold/matrix attachment regions (S/MARs) and is preceded by the degradation of nuclear proteins. The present study was performed to establish whether the same mechanism occurred in human NT2 cells subjected to oxygen and glucose deprivation (OGD). We analyzed the integrity of c-myc S/MAR containing a base-unpairing region (BUR)-like element, which we established to be a binding site of the transcription factor Sox2. An accumulation of DNA breaks in close proximity to this element and a degradation of Sox2 were observed early in the OGD-induced apoptotic response. Identification of Sox2 as a novel c-myc BUR-binding protein was achieved through yeast one-hybrid screening and the Sox2/DNA interaction was confirmed by electrophoretic mobility shift assay and immunoprecipitation with Sox2 antibody. Our data support the notion that early proteolysis of unique BUR-binding proteins might represent a universal mechanism that renders these DNA sites vulnerable to endonucleolysis. |
| doi_str_mv | 10.1038/sj.cdd.4401671 |
| format | Article |
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The present study was performed to establish whether the same mechanism occurred in human NT2 cells subjected to oxygen and glucose deprivation (OGD). We analyzed the integrity of c-myc S/MAR containing a base-unpairing region (BUR)-like element, which we established to be a binding site of the transcription factor Sox2. An accumulation of DNA breaks in close proximity to this element and a degradation of Sox2 were observed early in the OGD-induced apoptotic response. Identification of Sox2 as a novel c-myc BUR-binding protein was achieved through yeast one-hybrid screening and the Sox2/DNA interaction was confirmed by electrophoretic mobility shift assay and immunoprecipitation with Sox2 antibody. Our data support the notion that early proteolysis of unique BUR-binding proteins might represent a universal mechanism that renders these DNA sites vulnerable to endonucleolysis.</description><identifier>ISSN: 1350-9047</identifier><identifier>EISSN: 1476-5403</identifier><identifier>DOI: 10.1038/sj.cdd.4401671</identifier><identifier>PMID: 15920534</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Apoptosis ; Apoptosis - genetics ; Apoptosis - physiology ; Base Sequence ; Binding sites ; Biochemistry ; Biomedical and Life Sciences ; Carcinoma, Embryonal - genetics ; Carcinoma, Embryonal - metabolism ; Cell Biology ; Cell Cycle Analysis ; Cell death ; Cell Line, Tumor ; DNA Damage ; DNA, Neoplasm - genetics ; DNA, Neoplasm - metabolism ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Genes, myc - genetics ; Genes, myc - physiology ; Genomes ; HMGB Proteins - genetics ; HMGB Proteins - metabolism ; Humans ; Jurkat Cells ; Life Sciences ; Matrix Attachment Regions - genetics ; Matrix Attachment Regions - physiology ; Neurobiology ; Neurons - cytology ; Neurons - metabolism ; Neurosciences ; original-paper ; Polymerase Chain Reaction ; Proteins ; SOXB1 Transcription Factors ; Stem Cells ; Transcription factors ; Transcription Factors - genetics ; Transcription Factors - metabolism</subject><ispartof>Cell death and differentiation, 2005-11, Vol.12 (11), p.1368-1377</ispartof><rights>Springer Nature Limited 2005</rights><rights>Copyright Nature Publishing Group Nov 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c431t-6eb64e84b5e4503dc901d68cde69f16923ccde70d87de884272eaff36ae961bd3</citedby><cites>FETCH-LOGICAL-c431t-6eb64e84b5e4503dc901d68cde69f16923ccde70d87de884272eaff36ae961bd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/sj.cdd.4401671$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/sj.cdd.4401671$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51298</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15920534$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lei, J X</creatorcontrib><creatorcontrib>Liu, Q Y</creatorcontrib><creatorcontrib>Sodja, C</creatorcontrib><creatorcontrib>LeBlanc, J</creatorcontrib><creatorcontrib>Ribecco-Lutkiewicz, M</creatorcontrib><creatorcontrib>Smith, B</creatorcontrib><creatorcontrib>Charlebois, C</creatorcontrib><creatorcontrib>Walker, P R</creatorcontrib><creatorcontrib>Sikorska, M</creatorcontrib><title>S/MAR-binding properties of Sox2 and its involvement in apoptosis of human NT2 neural precursors</title><title>Cell death and differentiation</title><addtitle>Cell Death Differ</addtitle><addtitle>Cell Death Differ</addtitle><description>DNA fragmentation in apoptosis, especially in lymphocytic cells, is initiated at scaffold/matrix attachment regions (S/MARs) and is preceded by the degradation of nuclear proteins. 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Our data support the notion that early proteolysis of unique BUR-binding proteins might represent a universal mechanism that renders these DNA sites vulnerable to endonucleolysis.</description><subject>Apoptosis</subject><subject>Apoptosis - genetics</subject><subject>Apoptosis - physiology</subject><subject>Base Sequence</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Carcinoma, Embryonal - genetics</subject><subject>Carcinoma, Embryonal - metabolism</subject><subject>Cell Biology</subject><subject>Cell Cycle Analysis</subject><subject>Cell death</subject><subject>Cell Line, Tumor</subject><subject>DNA Damage</subject><subject>DNA, Neoplasm - genetics</subject><subject>DNA, Neoplasm - metabolism</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Genes, myc - genetics</subject><subject>Genes, myc - physiology</subject><subject>Genomes</subject><subject>HMGB Proteins - 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The present study was performed to establish whether the same mechanism occurred in human NT2 cells subjected to oxygen and glucose deprivation (OGD). We analyzed the integrity of c-myc S/MAR containing a base-unpairing region (BUR)-like element, which we established to be a binding site of the transcription factor Sox2. An accumulation of DNA breaks in close proximity to this element and a degradation of Sox2 were observed early in the OGD-induced apoptotic response. Identification of Sox2 as a novel c-myc BUR-binding protein was achieved through yeast one-hybrid screening and the Sox2/DNA interaction was confirmed by electrophoretic mobility shift assay and immunoprecipitation with Sox2 antibody. Our data support the notion that early proteolysis of unique BUR-binding proteins might represent a universal mechanism that renders these DNA sites vulnerable to endonucleolysis.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>15920534</pmid><doi>10.1038/sj.cdd.4401671</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Apoptosis Apoptosis - genetics Apoptosis - physiology Base Sequence Binding sites Biochemistry Biomedical and Life Sciences Carcinoma, Embryonal - genetics Carcinoma, Embryonal - metabolism Cell Biology Cell Cycle Analysis Cell death Cell Line, Tumor DNA Damage DNA, Neoplasm - genetics DNA, Neoplasm - metabolism DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Genes, myc - genetics Genes, myc - physiology Genomes HMGB Proteins - genetics HMGB Proteins - metabolism Humans Jurkat Cells Life Sciences Matrix Attachment Regions - genetics Matrix Attachment Regions - physiology Neurobiology Neurons - cytology Neurons - metabolism Neurosciences original-paper Polymerase Chain Reaction Proteins SOXB1 Transcription Factors Stem Cells Transcription factors Transcription Factors - genetics Transcription Factors - metabolism |
| title | S/MAR-binding properties of Sox2 and its involvement in apoptosis of human NT2 neural precursors |
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