Polypyrimidine tract binding protein and poly r(C) binding protein 1 interact with the BAG‐1 IRES and stimulate its activity in vitro and in vivo
The 5′‐untranslated region of Bag‐1 mRNA contains an internal ribosome entry segment (IRES) and the translation of Bag‐1 protein can be initiated by both cap‐dependent and cap‐independent mechanisms. In general, cellular IRESs require non‐canonical trans‐acting factors for their activity, however, v...
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| Veröffentlicht in: | Nucleic acids research 2003-01, Vol.31 (2), p.639-646 |
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| creator | Pickering, Becky M. Mitchell, Sally A. Evans, Joanne R. Willis, Anne E. |
| description | The 5′‐untranslated region of Bag‐1 mRNA contains an internal ribosome entry segment (IRES) and the translation of Bag‐1 protein can be initiated by both cap‐dependent and cap‐independent mechanisms. In general, cellular IRESs require non‐canonical trans‐acting factors for their activity, however, very few of the proteins that act on cellular IRESs have been identified. Proteins that interact with viral IRESs have also been shown to stimulate the activity of cellular IRESs and therefore the ability of a range of known viral trans‐acting factors to stimulate the Bag‐1 IRES was tested. Two proteins, poly r(C) binding protein 1 (PCBP1) and polypyrimidine tract binding protein (PTB), were found to increase the activity of the Bag‐1 IRES in vitro and in vivo. The regions of the Bag‐1 IRES RNA to which they bind have been determined, and it was shown that PCBP1 binds to a short 66 nt section of RNA, whilst PTB interacts with a number of sites over a larger area. The minimum section of the RNA that still retained activity was determined and both PCBP1 and PTB interacted with this region suggesting that these proteins are essential for Bag‐1 IRES function. |
| doi_str_mv | 10.1093/nar/gkg146 |
| format | Article |
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Acids Res</addtitle><description>The 5′‐untranslated region of Bag‐1 mRNA contains an internal ribosome entry segment (IRES) and the translation of Bag‐1 protein can be initiated by both cap‐dependent and cap‐independent mechanisms. In general, cellular IRESs require non‐canonical trans‐acting factors for their activity, however, very few of the proteins that act on cellular IRESs have been identified. Proteins that interact with viral IRESs have also been shown to stimulate the activity of cellular IRESs and therefore the ability of a range of known viral trans‐acting factors to stimulate the Bag‐1 IRES was tested. Two proteins, poly r(C) binding protein 1 (PCBP1) and polypyrimidine tract binding protein (PTB), were found to increase the activity of the Bag‐1 IRES in vitro and in vivo. The regions of the Bag‐1 IRES RNA to which they bind have been determined, and it was shown that PCBP1 binds to a short 66 nt section of RNA, whilst PTB interacts with a number of sites over a larger area. The minimum section of the RNA that still retained activity was determined and both PCBP1 and PTB interacted with this region suggesting that these proteins are essential for Bag‐1 IRES function.</description><subject>Animals</subject><subject>Binding Sites - genetics</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Line</subject><subject>COS Cells</subject><subject>DNA-Binding Proteins</subject><subject>Electrophoretic Mobility Shift Assay</subject><subject>HeLa Cells</subject><subject>Heterogeneous-Nuclear Ribonucleoproteins - genetics</subject><subject>Heterogeneous-Nuclear Ribonucleoproteins - metabolism</subject><subject>Humans</subject><subject>Luciferases - genetics</subject><subject>Luciferases - metabolism</subject><subject>Polypyrimidine Tract-Binding Protein - genetics</subject><subject>Polypyrimidine Tract-Binding Protein - metabolism</subject><subject>Protein Binding</subject><subject>Protein Biosynthesis</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Ribosomes - metabolism</subject><subject>RNA-Binding Proteins</subject><subject>Transcription Factors</subject><subject>Transcription, Genetic</subject><subject>Transfection</subject><subject>Tumor Cells, Cultured</subject><issn>0305-1048</issn><issn>1362-4962</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFks1uEzEUhUcIRNPChgdAFgtEkYb6-ndmwaKNSlMpgvInITaW4_Ekbiczg-0JZMcjIPGGPAluEpW_Baujq_sdy-fqZNkDwM8Al_So1f5ofjUHJm5lI6CC5KwU5HY2whTzHDAr9rL9EC4xBgac3c32gHAipSSj7PtF16z7tXdLV7nWoui1iWjm2jTNUe-7aF2LdFuhPoHIPxkf_rMF5NpoN8bPLi5QXFh0cnz24-s3QOdvTt9u7CG65dDoaJGLASXWrVxcJydK6rsNsxlW3b3sTq2bYO_v9CB7_-L03XiST1-dnY-Pp7lhGGI-00YaVhJRV0RTW9OZMSUTrKgklCxFLYiWnBpjq7oWgjAoNadJmKxoUWN6kD3fvtsPs6WtjG1T-kb16Rjar1Wnnfpz07qFmncrBQxzgOR_vPP77tNgQ1RLF4xtGt3abghKkrIACfi_IBRCcCGvwUd_gZfd4Nt0BEUwFgVgwhP0dAsZ34XgbX3zY8DquhAqFUJtC5Hgh79n_IXuGpCAfAu4EO2Xm732V0pIKrmafPio8JRNXr-8OFGc_gSoysN9</recordid><startdate>20030115</startdate><enddate>20030115</enddate><creator>Pickering, Becky M.</creator><creator>Mitchell, Sally A.</creator><creator>Evans, Joanne R.</creator><creator>Willis, Anne E.</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</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>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20030115</creationdate><title>Polypyrimidine tract binding protein and poly r(C) binding protein 1 interact with the BAG‐1 IRES and stimulate its activity in vitro and in vivo</title><author>Pickering, Becky M. ; Mitchell, Sally A. ; Evans, Joanne R. ; Willis, Anne E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-bac7c4926fd2a3ef3bcc94648d719414182a753ccedff662419a5324147d38f03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Binding Sites - genetics</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Line</topic><topic>COS Cells</topic><topic>DNA-Binding Proteins</topic><topic>Electrophoretic Mobility Shift Assay</topic><topic>HeLa Cells</topic><topic>Heterogeneous-Nuclear Ribonucleoproteins - genetics</topic><topic>Heterogeneous-Nuclear Ribonucleoproteins - metabolism</topic><topic>Humans</topic><topic>Luciferases - genetics</topic><topic>Luciferases - metabolism</topic><topic>Polypyrimidine Tract-Binding Protein - genetics</topic><topic>Polypyrimidine Tract-Binding Protein - metabolism</topic><topic>Protein Binding</topic><topic>Protein Biosynthesis</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Ribosomes - metabolism</topic><topic>RNA-Binding Proteins</topic><topic>Transcription Factors</topic><topic>Transcription, Genetic</topic><topic>Transfection</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pickering, Becky M.</creatorcontrib><creatorcontrib>Mitchell, Sally A.</creatorcontrib><creatorcontrib>Evans, Joanne R.</creatorcontrib><creatorcontrib>Willis, Anne E.</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids 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>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pickering, Becky M.</au><au>Mitchell, Sally A.</au><au>Evans, Joanne R.</au><au>Willis, Anne E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Polypyrimidine tract binding protein and poly r(C) binding protein 1 interact with the BAG‐1 IRES and stimulate its activity in vitro and in vivo</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucl. Acids Res</addtitle><date>2003-01-15</date><risdate>2003</risdate><volume>31</volume><issue>2</issue><spage>639</spage><epage>646</epage><pages>639-646</pages><issn>0305-1048</issn><issn>1362-4962</issn><eissn>1362-4962</eissn><coden>NARHAD</coden><abstract>The 5′‐untranslated region of Bag‐1 mRNA contains an internal ribosome entry segment (IRES) and the translation of Bag‐1 protein can be initiated by both cap‐dependent and cap‐independent mechanisms. In general, cellular IRESs require non‐canonical trans‐acting factors for their activity, however, very few of the proteins that act on cellular IRESs have been identified. Proteins that interact with viral IRESs have also been shown to stimulate the activity of cellular IRESs and therefore the ability of a range of known viral trans‐acting factors to stimulate the Bag‐1 IRES was tested. Two proteins, poly r(C) binding protein 1 (PCBP1) and polypyrimidine tract binding protein (PTB), were found to increase the activity of the Bag‐1 IRES in vitro and in vivo. The regions of the Bag‐1 IRES RNA to which they bind have been determined, and it was shown that PCBP1 binds to a short 66 nt section of RNA, whilst PTB interacts with a number of sites over a larger area. The minimum section of the RNA that still retained activity was determined and both PCBP1 and PTB interacted with this region suggesting that these proteins are essential for Bag‐1 IRES function.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>12527772</pmid><doi>10.1093/nar/gkg146</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Nucleic acids research, 2003-01, Vol.31 (2), p.639-646 |
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| subjects | Animals Binding Sites - genetics Carrier Proteins - genetics Carrier Proteins - metabolism Cell Line COS Cells DNA-Binding Proteins Electrophoretic Mobility Shift Assay HeLa Cells Heterogeneous-Nuclear Ribonucleoproteins - genetics Heterogeneous-Nuclear Ribonucleoproteins - metabolism Humans Luciferases - genetics Luciferases - metabolism Polypyrimidine Tract-Binding Protein - genetics Polypyrimidine Tract-Binding Protein - metabolism Protein Binding Protein Biosynthesis Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Ribosomes - metabolism RNA-Binding Proteins Transcription Factors Transcription, Genetic Transfection Tumor Cells, Cultured |
| title | Polypyrimidine tract binding protein and poly r(C) binding protein 1 interact with the BAG‐1 IRES and stimulate its activity in vitro and in vivo |
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