Purification and characterization of a heat stable nuclear factor CIIIB1 involved in the regulation of the human ApoC-III gene
The apoC-III promoter region -86 to -74 is recognized by two nuclear factors designated CIIIB1 and CIIIB2 (NF-BA1) which are both activators of apoC-III gene transcription (Ogami, K., Hadzopoulou-Cladaras, M., Cladaras, C., and Zannis, V. I. (1990) J. Biol. Chem. 265, 9808-9815). In this communicati...
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| Veröffentlicht in: | The Journal of biological chemistry 1991-05, Vol.266 (15), p.9640-9646 |
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| creator | OGAMI, K KARDASSIS, D CLADARAS, C ZANNIS, V. I |
| description | The apoC-III promoter region -86 to -74 is recognized by two nuclear factors designated CIIIB1 and CIIIB2 (NF-BA1) which are
both activators of apoC-III gene transcription (Ogami, K., Hadzopoulou-Cladaras, M., Cladaras, C., and Zannis, V. I. (1990)
J. Biol. Chem. 265, 9808-9815). In this communication we report the purification of factor CIIIB1 from rat liver nuclear extracts.
The purification procedure included anion- and cation-exchange chromatography, DNA sequence-specific affinity chromatography,
and heat treatment at 85 degrees C for 5 min. The ligand used for affinity chromatography was a mutated apoC-III -90 to -73
promoter sequence which binds only the CIIIB1 factor. The purified protein was identified as a poly-peptide of Mr 41,000 by
sodium dodecyl sulfate-polyacrylamide gel electrophoresis and photoaffinity cross-linking. The binding site of CIIIB1, defined
by DNase I footprinting and methylation interference assays, contains the octameric motif CAGGTGAC. Nucleotide substitutions
within this sequence abolished the binding of the purified factor. DNase I footprinting analysis showed that purified CIIIB1
protein protects the apoA-II promoter region -65 to -48 which contains an identical octameric CAGGTGAC motif in the antisense
strand suggesting that CIIIB1 may also play a role in apoA-II gene regulation. |
| doi_str_mv | 10.1016/S0021-9258(18)92868-1 |
| format | Article |
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both activators of apoC-III gene transcription (Ogami, K., Hadzopoulou-Cladaras, M., Cladaras, C., and Zannis, V. I. (1990)
J. Biol. Chem. 265, 9808-9815). In this communication we report the purification of factor CIIIB1 from rat liver nuclear extracts.
The purification procedure included anion- and cation-exchange chromatography, DNA sequence-specific affinity chromatography,
and heat treatment at 85 degrees C for 5 min. The ligand used for affinity chromatography was a mutated apoC-III -90 to -73
promoter sequence which binds only the CIIIB1 factor. The purified protein was identified as a poly-peptide of Mr 41,000 by
sodium dodecyl sulfate-polyacrylamide gel electrophoresis and photoaffinity cross-linking. The binding site of CIIIB1, defined
by DNase I footprinting and methylation interference assays, contains the octameric motif CAGGTGAC. Nucleotide substitutions
within this sequence abolished the binding of the purified factor. DNase I footprinting analysis showed that purified CIIIB1
protein protects the apoA-II promoter region -65 to -48 which contains an identical octameric CAGGTGAC motif in the antisense
strand suggesting that CIIIB1 may also play a role in apoA-II gene regulation.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)92868-1</identifier><identifier>PMID: 2033057</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Apolipoprotein C-III ; Apolipoproteins C - genetics ; Base Sequence ; Binding Sites ; Biological and medical sciences ; Cell physiology ; Chromatography, Liquid ; Cross-Linking Reagents ; DNA Fingerprinting ; DNA-Binding Proteins - metabolism ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation ; Humans ; Liver - metabolism ; Molecular and cellular biology ; Molecular Sequence Data ; Nuclear Proteins - chemistry ; Nuclear Proteins - isolation & purification ; Promoter Regions, Genetic ; Rats ; Responses to growth factors, tumor promotors, other factors ; Trans-Activators</subject><ispartof>The Journal of biological chemistry, 1991-05, Vol.266 (15), p.9640-9646</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-bc74da4ef9adc8c5641a7e0aed4f8a918cde9dd73214d77611802ae28c1e37b03</citedby><cites>FETCH-LOGICAL-c409t-bc74da4ef9adc8c5641a7e0aed4f8a918cde9dd73214d77611802ae28c1e37b03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19737658$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2033057$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>OGAMI, K</creatorcontrib><creatorcontrib>KARDASSIS, D</creatorcontrib><creatorcontrib>CLADARAS, C</creatorcontrib><creatorcontrib>ZANNIS, V. I</creatorcontrib><title>Purification and characterization of a heat stable nuclear factor CIIIB1 involved in the regulation of the human ApoC-III gene</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The apoC-III promoter region -86 to -74 is recognized by two nuclear factors designated CIIIB1 and CIIIB2 (NF-BA1) which are
both activators of apoC-III gene transcription (Ogami, K., Hadzopoulou-Cladaras, M., Cladaras, C., and Zannis, V. I. (1990)
J. Biol. Chem. 265, 9808-9815). In this communication we report the purification of factor CIIIB1 from rat liver nuclear extracts.
The purification procedure included anion- and cation-exchange chromatography, DNA sequence-specific affinity chromatography,
and heat treatment at 85 degrees C for 5 min. The ligand used for affinity chromatography was a mutated apoC-III -90 to -73
promoter sequence which binds only the CIIIB1 factor. The purified protein was identified as a poly-peptide of Mr 41,000 by
sodium dodecyl sulfate-polyacrylamide gel electrophoresis and photoaffinity cross-linking. The binding site of CIIIB1, defined
by DNase I footprinting and methylation interference assays, contains the octameric motif CAGGTGAC. Nucleotide substitutions
within this sequence abolished the binding of the purified factor. DNase I footprinting analysis showed that purified CIIIB1
protein protects the apoA-II promoter region -65 to -48 which contains an identical octameric CAGGTGAC motif in the antisense
strand suggesting that CIIIB1 may also play a role in apoA-II gene regulation.</description><subject>Animals</subject><subject>Apolipoprotein C-III</subject><subject>Apolipoproteins C - genetics</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Cell physiology</subject><subject>Chromatography, Liquid</subject><subject>Cross-Linking Reagents</subject><subject>DNA Fingerprinting</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation</subject><subject>Humans</subject><subject>Liver - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Nuclear Proteins - chemistry</subject><subject>Nuclear Proteins - isolation & purification</subject><subject>Promoter Regions, Genetic</subject><subject>Rats</subject><subject>Responses to growth factors, tumor promotors, other factors</subject><subject>Trans-Activators</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkF1rFDEUhoNY6lr9CYWAKHoxmjNfSS7bRe1CoYIK3oUzyZmdyMxkTWYq9sLf7mx3WXOTcM7zvoGHsUsQ70FA_eGrEDlkOq_UW1DvdK5qlcETtgKhiqyo4MdTtjohz9jzlH6K5ZQaztl5LopCVHLF_n6Zo2-9xcmHkePouO0wop0o-ofDMLQceUc48TRh0xMfZ9sTRt4uWIh8vdlsroH78T709-SWB5864pG2c39q2E-6ecCRX-3COlsifEsjvWBnLfaJXh7vC_b908dv65vs9u7zZn11m9lS6ClrrCwdltRqdFbZqi4BJQkkV7YKNSjrSDsnixxKJ2UNoESOlCsLVMhGFBfszaF3F8OvmdJkBp8s9T2OFOZklKjqSos9WB1AG0NKkVqzi37A-MeAMHvv5tG72Us1oMyjdwNL7vL4wdwM5E6po-hl__q4x2SxbyOO1qf_5VoWsq7Uwr06cJ3fdr99JNP4YDsaTF7XBiqj61IU_wAeG5d2</recordid><startdate>19910525</startdate><enddate>19910525</enddate><creator>OGAMI, K</creator><creator>KARDASSIS, D</creator><creator>CLADARAS, C</creator><creator>ZANNIS, V. I</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</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>7X8</scope></search><sort><creationdate>19910525</creationdate><title>Purification and characterization of a heat stable nuclear factor CIIIB1 involved in the regulation of the human ApoC-III gene</title><author>OGAMI, K ; KARDASSIS, D ; CLADARAS, C ; ZANNIS, V. I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-bc74da4ef9adc8c5641a7e0aed4f8a918cde9dd73214d77611802ae28c1e37b03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Animals</topic><topic>Apolipoprotein C-III</topic><topic>Apolipoproteins C - genetics</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Cell physiology</topic><topic>Chromatography, Liquid</topic><topic>Cross-Linking Reagents</topic><topic>DNA Fingerprinting</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation</topic><topic>Humans</topic><topic>Liver - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Nuclear Proteins - chemistry</topic><topic>Nuclear Proteins - isolation & purification</topic><topic>Promoter Regions, Genetic</topic><topic>Rats</topic><topic>Responses to growth factors, tumor promotors, other factors</topic><topic>Trans-Activators</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>OGAMI, K</creatorcontrib><creatorcontrib>KARDASSIS, D</creatorcontrib><creatorcontrib>CLADARAS, C</creatorcontrib><creatorcontrib>ZANNIS, V. I</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>OGAMI, K</au><au>KARDASSIS, D</au><au>CLADARAS, C</au><au>ZANNIS, V. I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of a heat stable nuclear factor CIIIB1 involved in the regulation of the human ApoC-III gene</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1991-05-25</date><risdate>1991</risdate><volume>266</volume><issue>15</issue><spage>9640</spage><epage>9646</epage><pages>9640-9646</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The apoC-III promoter region -86 to -74 is recognized by two nuclear factors designated CIIIB1 and CIIIB2 (NF-BA1) which are
both activators of apoC-III gene transcription (Ogami, K., Hadzopoulou-Cladaras, M., Cladaras, C., and Zannis, V. I. (1990)
J. Biol. Chem. 265, 9808-9815). In this communication we report the purification of factor CIIIB1 from rat liver nuclear extracts.
The purification procedure included anion- and cation-exchange chromatography, DNA sequence-specific affinity chromatography,
and heat treatment at 85 degrees C for 5 min. The ligand used for affinity chromatography was a mutated apoC-III -90 to -73
promoter sequence which binds only the CIIIB1 factor. The purified protein was identified as a poly-peptide of Mr 41,000 by
sodium dodecyl sulfate-polyacrylamide gel electrophoresis and photoaffinity cross-linking. The binding site of CIIIB1, defined
by DNase I footprinting and methylation interference assays, contains the octameric motif CAGGTGAC. Nucleotide substitutions
within this sequence abolished the binding of the purified factor. DNase I footprinting analysis showed that purified CIIIB1
protein protects the apoA-II promoter region -65 to -48 which contains an identical octameric CAGGTGAC motif in the antisense
strand suggesting that CIIIB1 may also play a role in apoA-II gene regulation.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2033057</pmid><doi>10.1016/S0021-9258(18)92868-1</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Apolipoprotein C-III Apolipoproteins C - genetics Base Sequence Binding Sites Biological and medical sciences Cell physiology Chromatography, Liquid Cross-Linking Reagents DNA Fingerprinting DNA-Binding Proteins - metabolism Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Gene Expression Regulation Humans Liver - metabolism Molecular and cellular biology Molecular Sequence Data Nuclear Proteins - chemistry Nuclear Proteins - isolation & purification Promoter Regions, Genetic Rats Responses to growth factors, tumor promotors, other factors Trans-Activators |
| title | Purification and characterization of a heat stable nuclear factor CIIIB1 involved in the regulation of the human ApoC-III gene |
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