Back-priming mode of phi6 RNA-dependent RNA polymerase.
The RNA-dependent RNA polymerase of the double-stranded RNA bacteriophage phi6 is capable of primer-independent initiation, as are many RNA polymerases. The structure of this polymerase revealed an initiation platform, composed of a loop in the C-terminal domain (QYKW, aa 629-632), that was essentia...
| Autors principals: | , , , , |
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| Format: | Journal article |
| Idioma: | English |
| Publicat: |
2005
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| _version_ | 1826258372146495488 |
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| author | Laurila, MR Salgado, P Stuart, D Grimes, J Bamford, D |
| author_facet | Laurila, MR Salgado, P Stuart, D Grimes, J Bamford, D |
| author_sort | Laurila, MR |
| collection | OXFORD |
| description | The RNA-dependent RNA polymerase of the double-stranded RNA bacteriophage phi6 is capable of primer-independent initiation, as are many RNA polymerases. The structure of this polymerase revealed an initiation platform, composed of a loop in the C-terminal domain (QYKW, aa 629-632), that was essential for de novo initiation. A similar element has been identified in hepatitis C virus RNA-dependent RNA polymerase. Biochemical studies have addressed the role of this platform, revealing that a mutant version can utilize a back-priming initiation mechanism, where the 3' terminus of the template adopts a hairpin-like conformation. Here, the mechanism of back-primed initiation is studied further by biochemical and structural methods. |
| first_indexed | 2024-03-06T18:32:57Z |
| format | Journal article |
| id | oxford-uuid:0a446d52-d5a9-40f1-89de-e3042d8c1547 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:32:57Z |
| publishDate | 2005 |
| record_format | dspace |
| spelling | oxford-uuid:0a446d52-d5a9-40f1-89de-e3042d8c15472022-03-26T09:23:00ZBack-priming mode of phi6 RNA-dependent RNA polymerase.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:0a446d52-d5a9-40f1-89de-e3042d8c1547EnglishSymplectic Elements at Oxford2005Laurila, MRSalgado, PStuart, DGrimes, JBamford, DThe RNA-dependent RNA polymerase of the double-stranded RNA bacteriophage phi6 is capable of primer-independent initiation, as are many RNA polymerases. The structure of this polymerase revealed an initiation platform, composed of a loop in the C-terminal domain (QYKW, aa 629-632), that was essential for de novo initiation. A similar element has been identified in hepatitis C virus RNA-dependent RNA polymerase. Biochemical studies have addressed the role of this platform, revealing that a mutant version can utilize a back-priming initiation mechanism, where the 3' terminus of the template adopts a hairpin-like conformation. Here, the mechanism of back-primed initiation is studied further by biochemical and structural methods. |
| spellingShingle | Laurila, MR Salgado, P Stuart, D Grimes, J Bamford, D Back-priming mode of phi6 RNA-dependent RNA polymerase. |
| title | Back-priming mode of phi6 RNA-dependent RNA polymerase. |
| title_full | Back-priming mode of phi6 RNA-dependent RNA polymerase. |
| title_fullStr | Back-priming mode of phi6 RNA-dependent RNA polymerase. |
| title_full_unstemmed | Back-priming mode of phi6 RNA-dependent RNA polymerase. |
| title_short | Back-priming mode of phi6 RNA-dependent RNA polymerase. |
| title_sort | back priming mode of phi6 rna dependent rna polymerase |
| work_keys_str_mv | AT laurilamr backprimingmodeofphi6rnadependentrnapolymerase AT salgadop backprimingmodeofphi6rnadependentrnapolymerase AT stuartd backprimingmodeofphi6rnadependentrnapolymerase AT grimesj backprimingmodeofphi6rnadependentrnapolymerase AT bamfordd backprimingmodeofphi6rnadependentrnapolymerase |