The C-terminal priming domain is strongly associated with the main body of bacteriophage ϕ6 RNA-dependent RNA polymerase.
Double-stranded RNA viruses encode a single protein species containing RNA-dependent RNA polymerase (RdRP) motifs. This protein is responsible for RNA transcription and replication. The architecture of viral RdRPs resembles that of a cupped right hand with fingers, palm and thumb domains. Those usin...
| Main Authors: | , , , , , , , |
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| 格式: | Journal article |
| 语言: | English |
| 出版: |
2012
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| _version_ | 1826289067126423552 |
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| author | Sarin, L Wright, S Chen, Q Degerth, L Stuart, D Grimes, J Bamford, D Poranen, M |
| author_facet | Sarin, L Wright, S Chen, Q Degerth, L Stuart, D Grimes, J Bamford, D Poranen, M |
| author_sort | Sarin, L |
| collection | OXFORD |
| description | Double-stranded RNA viruses encode a single protein species containing RNA-dependent RNA polymerase (RdRP) motifs. This protein is responsible for RNA transcription and replication. The architecture of viral RdRPs resembles that of a cupped right hand with fingers, palm and thumb domains. Those using de novo initiation have a flexible structural elaboration that constitutes the priming platform. Here we investigate the properties of the C-terminal priming domain of bacteriophage ϕ6 to get insights into the role of an extended loop connecting this domain to the main body of the polymerase. Proteolyzed ϕ6 RdRP that possesses a nick in the hinge region of this loop was better suited for de novo initiation. The clipped C-terminus remained associated with the main body of the polymerase via the anchor helix. The structurally flexible hinge region appeared to be involved in the control of priming platform movement. Moreover, we detected abortive initiation products for a bacteriophage RdRP. |
| first_indexed | 2024-03-07T02:23:15Z |
| format | Journal article |
| id | oxford-uuid:a4aebb51-d77e-4c23-ae67-d14350a884bd |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:23:15Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:a4aebb51-d77e-4c23-ae67-d14350a884bd2022-03-27T02:35:32ZThe C-terminal priming domain is strongly associated with the main body of bacteriophage ϕ6 RNA-dependent RNA polymerase.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:a4aebb51-d77e-4c23-ae67-d14350a884bdEnglishSymplectic Elements at Oxford2012Sarin, LWright, SChen, QDegerth, LStuart, DGrimes, JBamford, DPoranen, MDouble-stranded RNA viruses encode a single protein species containing RNA-dependent RNA polymerase (RdRP) motifs. This protein is responsible for RNA transcription and replication. The architecture of viral RdRPs resembles that of a cupped right hand with fingers, palm and thumb domains. Those using de novo initiation have a flexible structural elaboration that constitutes the priming platform. Here we investigate the properties of the C-terminal priming domain of bacteriophage ϕ6 to get insights into the role of an extended loop connecting this domain to the main body of the polymerase. Proteolyzed ϕ6 RdRP that possesses a nick in the hinge region of this loop was better suited for de novo initiation. The clipped C-terminus remained associated with the main body of the polymerase via the anchor helix. The structurally flexible hinge region appeared to be involved in the control of priming platform movement. Moreover, we detected abortive initiation products for a bacteriophage RdRP. |
| spellingShingle | Sarin, L Wright, S Chen, Q Degerth, L Stuart, D Grimes, J Bamford, D Poranen, M The C-terminal priming domain is strongly associated with the main body of bacteriophage ϕ6 RNA-dependent RNA polymerase. |
| title | The C-terminal priming domain is strongly associated with the main body of bacteriophage ϕ6 RNA-dependent RNA polymerase. |
| title_full | The C-terminal priming domain is strongly associated with the main body of bacteriophage ϕ6 RNA-dependent RNA polymerase. |
| title_fullStr | The C-terminal priming domain is strongly associated with the main body of bacteriophage ϕ6 RNA-dependent RNA polymerase. |
| title_full_unstemmed | The C-terminal priming domain is strongly associated with the main body of bacteriophage ϕ6 RNA-dependent RNA polymerase. |
| title_short | The C-terminal priming domain is strongly associated with the main body of bacteriophage ϕ6 RNA-dependent RNA polymerase. |
| title_sort | c terminal priming domain is strongly associated with the main body of bacteriophage ϕ6 rna dependent rna polymerase |
| work_keys_str_mv | AT sarinl thecterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT wrights thecterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT chenq thecterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT degerthl thecterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT stuartd thecterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT grimesj thecterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT bamfordd thecterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT poranenm thecterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT sarinl cterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT wrights cterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT chenq cterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT degerthl cterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT stuartd cterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT grimesj cterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT bamfordd cterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase AT poranenm cterminalprimingdomainisstronglyassociatedwiththemainbodyofbacteriophageph6rnadependentrnapolymerase |