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Keywords {🔍}

journals, open, sciences, permissions, access, search, ires, page, taylor, francis, journal, studies, browse, rna, find, environment, science, information, article, articles, group, publish, health, social, technology, register, mutations, reprints, mutant, rnas, corporate, content, close, menu, select, calls, papers, suggester, publishing, guidance, author, services, bioscience, earth, engineering, humanities, medicine, physical, crossref, citations,

Topics {✒️}

social care medicine hnrnp c1/c2 binds hnrnp c1/c2 protein cytoplasmic trans-acting factors francis group twitter page taylor request academic permissions journal search calls bind mutant rnas p53-ires rnas find guidance receive personalised research p53 ires rna p53- ires rna journals books crossref citations journals browse citing articles based author services home nuclease mapping experiments decreased ires activities obtain permissions instantly provide access putative secondary structure read lists articles enhancing ires function wild-type rna corporate permissions cart search mutant rnas reprints similar extent compared view content journals a open date register p53-ires p53 ires consequent decrease crossref icon obtain permissions p53 isoform register log issues volume 8 issue 1 effect information secondary structure ires function selecting permissions permissions form

Questions {❓}

• Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
• Why publish with us?

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            name:Effect of mutations on the p53 IRES RNA ....
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      name:Effect of mutations on the p53 IRES RNA structure: Implications for de-regulation of the synthesis of p53 isoforms
      headline:Effect of mutations on the p53 IRES RNA structure: Implications for de-regulation of the synthesis of p53 isoforms
      abstract:Earlier we have demonstrated the presence of internal ribosome entry site (IRES) within tumor suppressor p53 mRNA. Here we have mapped the putative secondary structure of p53- IRES RNA using information from chemical probing and nuclease mapping experiments. Additionally, the secondary structure of the IRES element of the wild-type RNA was compared with cancer-derived silent mutant p53 RNAs. These mutations might result in the conformational alterations of p53-IRES RNAs. The results also indicate decreased IRES activities of the mutants as compared to wild-type RNA. Further, it was observed that some of the cytoplasmic trans-acting factors, critical for enhancing IRES function, were unable to bind mutant RNAs as efficiently as to wild-type. Our results suggest that hnRNP C1/C2 binds to p53-IRES and siRNA mediated partial silencing of hnRNP C1/C2 showed appreciable decrease in IRES function and consequent decrease in the level of the corresponding p53 isoform. Interestingly mutant p53 IRES showed lesser binding with hnRNP C1/C2 protein. Finally, upon doxorubicin treatment, the mutant RNAs were unable to show enhanced p53 synthesis to similar extent compared to wild type. Taken together, these observations suggest that mutations occurring in the p53 IRES might have profound implications for de-regulation of its expression and activity.
      description:Earlier we have demonstrated the presence of internal ribosome entry site (IRES) within tumor suppressor p53 mRNA. Here we have mapped the putative secondary structure of p53- IRES RNA using information from chemical probing and nuclease mapping experiments. Additionally, the secondary structure of the IRES element of the wild-type RNA was compared with cancer-derived silent mutant p53 RNAs. These mutations might result in the conformational alterations of p53-IRES RNAs. The results also indicate decreased IRES activities of the mutants as compared to wild-type RNA. Further, it was observed that some of the cytoplasmic trans-acting factors, critical for enhancing IRES function, were unable to bind mutant RNAs as efficiently as to wild-type. Our results suggest that hnRNP C1/C2 binds to p53-IRES and siRNA mediated partial silencing of hnRNP C1/C2 showed appreciable decrease in IRES function and consequent decrease in the level of the corresponding p53 isoform. Interestingly mutant p53 IRES showed lesser binding with hnRNP C1/C2 protein. Finally, upon doxorubicin treatment, the mutant RNAs were unable to show enhanced p53 synthesis to similar extent compared to wild type. Taken together, these observations suggest that mutations occurring in the p53 IRES might have profound implications for de-regulation of its expression and activity.
      author:
            type:Person
            name:Anand Ponnuswamy
            type:Person
            name:Richa Grover
            type:Person
            name:Debjit Khan
            type:Person
            name:Arandkar Sharathchandra
            type:Person
            name:Saumitra Das
            type:Person
            name:Saumitra Das
      pageStart:132
      pageEnd:142
      datePublished:2011-01-01
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