Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex.
The influenza A virus RNA-dependent RNA polymerase is a heterotrimeric complex of polymerase basic protein 1 (PB1), PB2, and polymerase acidic protein (PA) subunits. It performs transcription and replication of the viral RNA genome in the nucleus of infected cells. We have identified a nuclear impor...
Главные авторы: | , , , , , |
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Формат: | Journal article |
Язык: | English |
Опубликовано: |
2006
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_version_ | 1826295968816955392 |
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author | Deng, T Engelhardt, O Thomas, B Akoulitchev, A Brownlee, G Fodor, E |
author_facet | Deng, T Engelhardt, O Thomas, B Akoulitchev, A Brownlee, G Fodor, E |
author_sort | Deng, T |
collection | OXFORD |
description | The influenza A virus RNA-dependent RNA polymerase is a heterotrimeric complex of polymerase basic protein 1 (PB1), PB2, and polymerase acidic protein (PA) subunits. It performs transcription and replication of the viral RNA genome in the nucleus of infected cells. We have identified a nuclear import factor, Ran binding protein 5 (RanBP5), also known as karyopherin beta3, importin beta3, or importin 5, as an interactor of the PB1 subunit. RanBP5 interacted with either PB1 alone or with a PB1-PA dimer but not with a PB1-PB2 dimer or the trimeric complex. The interaction between RanBP5 and PB1-PA was disrupted by RanGTP in vitro, allowing PB2 to bind to the PB1-PA dimer to form a functional trimeric RNA polymerase complex. We propose a model in which RanBP5 acts as an import factor for the newly synthesized polymerase by targeting the PB1-PA dimer to the nucleus. In agreement with this model, small interfering RNA (siRNA)-mediated knock-down of RanBP5 inhibited the nuclear accumulation of the PB1-PA dimer. Moreover, siRNA knock-down of RanBP5 resulted in the delayed accumulation of viral RNAs in infected cells, confirming that RanBP5 plays a biological role during the influenza virus life cycle. |
first_indexed | 2024-03-07T04:09:08Z |
format | Journal article |
id | oxford-uuid:c73b09c0-633c-4c1c-bf93-2c68b3c348c1 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T04:09:08Z |
publishDate | 2006 |
record_format | dspace |
spelling | oxford-uuid:c73b09c0-633c-4c1c-bf93-2c68b3c348c12022-03-27T06:43:29ZRole of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:c73b09c0-633c-4c1c-bf93-2c68b3c348c1EnglishSymplectic Elements at Oxford2006Deng, TEngelhardt, OThomas, BAkoulitchev, ABrownlee, GFodor, EThe influenza A virus RNA-dependent RNA polymerase is a heterotrimeric complex of polymerase basic protein 1 (PB1), PB2, and polymerase acidic protein (PA) subunits. It performs transcription and replication of the viral RNA genome in the nucleus of infected cells. We have identified a nuclear import factor, Ran binding protein 5 (RanBP5), also known as karyopherin beta3, importin beta3, or importin 5, as an interactor of the PB1 subunit. RanBP5 interacted with either PB1 alone or with a PB1-PA dimer but not with a PB1-PB2 dimer or the trimeric complex. The interaction between RanBP5 and PB1-PA was disrupted by RanGTP in vitro, allowing PB2 to bind to the PB1-PA dimer to form a functional trimeric RNA polymerase complex. We propose a model in which RanBP5 acts as an import factor for the newly synthesized polymerase by targeting the PB1-PA dimer to the nucleus. In agreement with this model, small interfering RNA (siRNA)-mediated knock-down of RanBP5 inhibited the nuclear accumulation of the PB1-PA dimer. Moreover, siRNA knock-down of RanBP5 resulted in the delayed accumulation of viral RNAs in infected cells, confirming that RanBP5 plays a biological role during the influenza virus life cycle. |
spellingShingle | Deng, T Engelhardt, O Thomas, B Akoulitchev, A Brownlee, G Fodor, E Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex. |
title | Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex. |
title_full | Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex. |
title_fullStr | Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex. |
title_full_unstemmed | Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex. |
title_short | Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex. |
title_sort | role of ran binding protein 5 in nuclear import and assembly of the influenza virus rna polymerase complex |
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