The p53 Protein is an Unusually Shaped Tetramer that Binds Directly to DNA
We have analyzed the size and structure of native immunopurified human p53 protein. By using a combination of chemical crosslinking, gel filtration chromatography, and zonal velocity gradient centrifugation, we have determined that the predominant form of p53 in such preparations is a tetramer. The...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1993-04, Vol.90 (8), p.3319-3323 |
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| creator | Friedman, Paula N. Chen, Xinbin Bargonetti, Jill Prives, Carol |
| description | We have analyzed the size and structure of native immunopurified human p53 protein. By using a combination of chemical crosslinking, gel filtration chromatography, and zonal velocity gradient centrifugation, we have determined that the predominant form of p53 in such preparations is a tetramer. The behavior of purified p53 in gels and sucrose gradients implies that the protein has an extended shape. Wild-type p53 has been shown to bind specifically to sites in cellular and viral DNA. We show in this study by Southwestern ligand blotting and by analysis of DNA-bound crosslinked p53 that p53 monomers, dimers, and tetramers can bind directly to DNA. |
| doi_str_mv | 10.1073/pnas.90.8.3319 |
| format | Article |
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By using a combination of chemical crosslinking, gel filtration chromatography, and zonal velocity gradient centrifugation, we have determined that the predominant form of p53 in such preparations is a tetramer. The behavior of purified p53 in gels and sucrose gradients implies that the protein has an extended shape. Wild-type p53 has been shown to bind specifically to sites in cellular and viral DNA. We show in this study by Southwestern ligand blotting and by analysis of DNA-bound crosslinked p53 that p53 monomers, dimers, and tetramers can bind directly to DNA.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.90.8.3319</identifier><identifier>PMID: 8475074</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Baculoviridae - genetics ; Biochemistry ; Biological and medical sciences ; Cancer ; Cell Line ; Centrifugation ; Centrifugation, Density Gradient ; Chromatography, Gel ; Cross-Linking Reagents ; Crosslinking ; Deoxyribonucleic acid ; Dimers ; DNA ; DNA - metabolism ; DNA, Viral - metabolism ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - isolation & purification ; DNA-Binding Proteins - metabolism ; Electrophoresis, Polyacrylamide Gel ; Elution ; Fundamental and applied biological sciences. Psychology ; Gels ; Glutaral ; Histidine ; Holoproteins ; Humans ; Macromolecular Substances ; Monomers ; Moths ; Mutagenesis, Site-Directed ; Nuclear proteins ; Oligodeoxyribonucleotides - metabolism ; Oligonucleotides ; Proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Transfection ; Tumor Suppressor Protein p53 - chemistry ; Tumor Suppressor Protein p53 - isolation & purification ; Tumor Suppressor Protein p53 - metabolism ; X ray film</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1993-04, Vol.90 (8), p.3319-3323</ispartof><rights>Copyright 1993 The National Academy of Sciences of the United States of America</rights><rights>1993 INIST-CNRS</rights><rights>Copyright National Academy of Sciences Apr 15, 1993</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c544t-42fb3ec02c4fe4d126cdd731891f17c9bfcdf4769c6526316f20a527edc374663</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/90/8.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2361735$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2361735$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4757008$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8475074$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Friedman, Paula N.</creatorcontrib><creatorcontrib>Chen, Xinbin</creatorcontrib><creatorcontrib>Bargonetti, Jill</creatorcontrib><creatorcontrib>Prives, Carol</creatorcontrib><title>The p53 Protein is an Unusually Shaped Tetramer that Binds Directly to DNA</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>We have analyzed the size and structure of native immunopurified human p53 protein. By using a combination of chemical crosslinking, gel filtration chromatography, and zonal velocity gradient centrifugation, we have determined that the predominant form of p53 in such preparations is a tetramer. The behavior of purified p53 in gels and sucrose gradients implies that the protein has an extended shape. Wild-type p53 has been shown to bind specifically to sites in cellular and viral DNA. We show in this study by Southwestern ligand blotting and by analysis of DNA-bound crosslinked p53 that p53 monomers, dimers, and tetramers can bind directly to DNA.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Baculoviridae - genetics</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cancer</subject><subject>Cell Line</subject><subject>Centrifugation</subject><subject>Centrifugation, Density Gradient</subject><subject>Chromatography, Gel</subject><subject>Cross-Linking Reagents</subject><subject>Crosslinking</subject><subject>Deoxyribonucleic acid</subject><subject>Dimers</subject><subject>DNA</subject><subject>DNA - metabolism</subject><subject>DNA, Viral - metabolism</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - isolation & purification</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Elution</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>Glutaral</subject><subject>Histidine</subject><subject>Holoproteins</subject><subject>Humans</subject><subject>Macromolecular Substances</subject><subject>Monomers</subject><subject>Moths</subject><subject>Mutagenesis, Site-Directed</subject><subject>Nuclear proteins</subject><subject>Oligodeoxyribonucleotides - metabolism</subject><subject>Oligonucleotides</subject><subject>Proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Transfection</subject><subject>Tumor Suppressor Protein p53 - chemistry</subject><subject>Tumor Suppressor Protein p53 - isolation & purification</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><subject>X ray film</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkUuLFDEUhYMoYzu6daUQRNxVmVflAbMZZ3wyqGDPOqRTiV1NdapMUuL8e1N0W7TiKpDznXvP5QDwFKMaI0Ffj8GkWqFa1pRidQ-sMFK44kyh-2CFEBGVZIQ9BI9S2iGEVCPRGTiTTDRIsBX4tN46ODYUfo1Ddl2AXYImwNswpcn0_R38tjWja-Ha5Wj2LsK8NRm-6UKb4HUXnc2FyQO8_nz5GDzwpk_uyfE9B7fv3q6vPlQ3X95_vLq8qWzDWK4Y8RvqLCKWecdaTLhtW0GxVNhjYdXG29YzwZXlDeEUc0-QaYhwraWCcU7PwcVh7jht9uXXhRKt12Ps9ibe6cF0-m8ldFv9ffipGScKF_uroz0OPyaXst53ybq-N8ENU9KYMyllM4Mv_gF3wxRDOU0ThIkQvJEFqg-QjUNK0fklB0Z6LkjPBWmFtNRzQcXw_DT9gh8bKfrLo26SNb2PJtguLVihBELy5Ip5_B91WaP91PfZ_con-_4LFv3ZQd-lPMQFIJRjQRv6G6lhuOU</recordid><startdate>19930415</startdate><enddate>19930415</enddate><creator>Friedman, Paula N.</creator><creator>Chen, Xinbin</creator><creator>Bargonetti, Jill</creator><creator>Prives, Carol</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>19930415</creationdate><title>The p53 Protein is an Unusually Shaped Tetramer that Binds Directly to DNA</title><author>Friedman, Paula N. ; Chen, Xinbin ; Bargonetti, Jill ; Prives, Carol</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c544t-42fb3ec02c4fe4d126cdd731891f17c9bfcdf4769c6526316f20a527edc374663</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Baculoviridae - genetics</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cancer</topic><topic>Cell Line</topic><topic>Centrifugation</topic><topic>Centrifugation, Density Gradient</topic><topic>Chromatography, Gel</topic><topic>Cross-Linking Reagents</topic><topic>Crosslinking</topic><topic>Deoxyribonucleic acid</topic><topic>Dimers</topic><topic>DNA</topic><topic>DNA - metabolism</topic><topic>DNA, Viral - metabolism</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - isolation & purification</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Elution</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>Glutaral</topic><topic>Histidine</topic><topic>Holoproteins</topic><topic>Humans</topic><topic>Macromolecular Substances</topic><topic>Monomers</topic><topic>Moths</topic><topic>Mutagenesis, Site-Directed</topic><topic>Nuclear proteins</topic><topic>Oligodeoxyribonucleotides - metabolism</topic><topic>Oligonucleotides</topic><topic>Proteins</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Transfection</topic><topic>Tumor Suppressor Protein p53 - chemistry</topic><topic>Tumor Suppressor Protein p53 - isolation & purification</topic><topic>Tumor Suppressor Protein p53 - metabolism</topic><topic>X ray film</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Friedman, Paula N.</creatorcontrib><creatorcontrib>Chen, Xinbin</creatorcontrib><creatorcontrib>Bargonetti, Jill</creatorcontrib><creatorcontrib>Prives, Carol</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>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Friedman, Paula N.</au><au>Chen, Xinbin</au><au>Bargonetti, Jill</au><au>Prives, Carol</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The p53 Protein is an Unusually Shaped Tetramer that Binds Directly to DNA</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1993-04-15</date><risdate>1993</risdate><volume>90</volume><issue>8</issue><spage>3319</spage><epage>3323</epage><pages>3319-3323</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>We have analyzed the size and structure of native immunopurified human p53 protein. By using a combination of chemical crosslinking, gel filtration chromatography, and zonal velocity gradient centrifugation, we have determined that the predominant form of p53 in such preparations is a tetramer. The behavior of purified p53 in gels and sucrose gradients implies that the protein has an extended shape. Wild-type p53 has been shown to bind specifically to sites in cellular and viral DNA. We show in this study by Southwestern ligand blotting and by analysis of DNA-bound crosslinked p53 that p53 monomers, dimers, and tetramers can bind directly to DNA.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8475074</pmid><doi>10.1073/pnas.90.8.3319</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1993-04, Vol.90 (8), p.3319-3323 |
| issn | 0027-8424 1091-6490 |
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| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Baculoviridae - genetics Biochemistry Biological and medical sciences Cancer Cell Line Centrifugation Centrifugation, Density Gradient Chromatography, Gel Cross-Linking Reagents Crosslinking Deoxyribonucleic acid Dimers DNA DNA - metabolism DNA, Viral - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - isolation & purification DNA-Binding Proteins - metabolism Electrophoresis, Polyacrylamide Gel Elution Fundamental and applied biological sciences. Psychology Gels Glutaral Histidine Holoproteins Humans Macromolecular Substances Monomers Moths Mutagenesis, Site-Directed Nuclear proteins Oligodeoxyribonucleotides - metabolism Oligonucleotides Proteins Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Transfection Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - isolation & purification Tumor Suppressor Protein p53 - metabolism X ray film |
| title | The p53 Protein is an Unusually Shaped Tetramer that Binds Directly to DNA |
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