Influenza virus inhibits RNA polymerase II elongation.
The influenza virus RNA-dependent RNA polymerase interacts with the serine-5 phosphorylated carboxy-terminal domain (CTD) of the large subunit of RNA polymerase II (Pol II). It was proposed that this interaction allows the viral RNA polymerase to gain access to host mRNA-derived capped RNA fragments...
| Auteurs principaux: | , , , , |
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| Format: | Journal article |
| Langue: | English |
| Publié: |
2006
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| _version_ | 1826271874220294144 |
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| author | Chan, A Vreede, F Smith, M Engelhardt, O Fodor, E |
| author_facet | Chan, A Vreede, F Smith, M Engelhardt, O Fodor, E |
| author_sort | Chan, A |
| collection | OXFORD |
| description | The influenza virus RNA-dependent RNA polymerase interacts with the serine-5 phosphorylated carboxy-terminal domain (CTD) of the large subunit of RNA polymerase II (Pol II). It was proposed that this interaction allows the viral RNA polymerase to gain access to host mRNA-derived capped RNA fragments required as primers for the initiation of viral mRNA synthesis. Here, we show, using a chromatin immunoprecipitation (ChIP) analysis, that similar amounts of Pol II associate with Pol II promoter DNAs in influenza virus-infected and mock-infected cells. However, there is a statistically significant reduction in Pol II densities in the coding region of Pol II genes in infected cells. Thus, influenza virus specifically interferes with Pol II elongation, but not Pol II initiation. We propose that influenza virus RNA polymerase, by binding to the CTD of initiating Pol II and subsequent cleavage of the capped 5' end of the nascent transcript, triggers premature Pol II termination. |
| first_indexed | 2024-03-06T22:03:37Z |
| format | Journal article |
| id | oxford-uuid:4f6a875c-96de-48f7-a3ce-a4937e6b0de9 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:03:37Z |
| publishDate | 2006 |
| record_format | dspace |
| spelling | oxford-uuid:4f6a875c-96de-48f7-a3ce-a4937e6b0de92022-03-26T16:07:05ZInfluenza virus inhibits RNA polymerase II elongation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4f6a875c-96de-48f7-a3ce-a4937e6b0de9EnglishSymplectic Elements at Oxford2006Chan, AVreede, FSmith, MEngelhardt, OFodor, EThe influenza virus RNA-dependent RNA polymerase interacts with the serine-5 phosphorylated carboxy-terminal domain (CTD) of the large subunit of RNA polymerase II (Pol II). It was proposed that this interaction allows the viral RNA polymerase to gain access to host mRNA-derived capped RNA fragments required as primers for the initiation of viral mRNA synthesis. Here, we show, using a chromatin immunoprecipitation (ChIP) analysis, that similar amounts of Pol II associate with Pol II promoter DNAs in influenza virus-infected and mock-infected cells. However, there is a statistically significant reduction in Pol II densities in the coding region of Pol II genes in infected cells. Thus, influenza virus specifically interferes with Pol II elongation, but not Pol II initiation. We propose that influenza virus RNA polymerase, by binding to the CTD of initiating Pol II and subsequent cleavage of the capped 5' end of the nascent transcript, triggers premature Pol II termination. |
| spellingShingle | Chan, A Vreede, F Smith, M Engelhardt, O Fodor, E Influenza virus inhibits RNA polymerase II elongation. |
| title | Influenza virus inhibits RNA polymerase II elongation. |
| title_full | Influenza virus inhibits RNA polymerase II elongation. |
| title_fullStr | Influenza virus inhibits RNA polymerase II elongation. |
| title_full_unstemmed | Influenza virus inhibits RNA polymerase II elongation. |
| title_short | Influenza virus inhibits RNA polymerase II elongation. |
| title_sort | influenza virus inhibits rna polymerase ii elongation |
| work_keys_str_mv | AT chana influenzavirusinhibitsrnapolymeraseiielongation AT vreedef influenzavirusinhibitsrnapolymeraseiielongation AT smithm influenzavirusinhibitsrnapolymeraseiielongation AT engelhardto influenzavirusinhibitsrnapolymeraseiielongation AT fodore influenzavirusinhibitsrnapolymeraseiielongation |