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TitleIn situ structures of rotavirus polymerase in action and mechanism of mRNA transcription and release.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 2216-2216, Year 2019
Publish dateMay 17, 2019
AuthorsKe Ding / Cristina C Celma / Xing Zhang / Thomas Chang / Wesley Shen / Ivo Atanasov / Polly Roy / Z Hong Zhou /
PubMed AbstractTranscribing and replicating a double-stranded genome require protein modules to unwind, transcribe/replicate nucleic acid substrates, and release products. Here we present in situ cryo-electron ...Transcribing and replicating a double-stranded genome require protein modules to unwind, transcribe/replicate nucleic acid substrates, and release products. Here we present in situ cryo-electron microscopy structures of rotavirus dsRNA-dependent RNA polymerase (RdRp) in two states pertaining to transcription. In addition to the previously discovered universal "hand-shaped" polymerase core domain shared by DNA polymerases and telomerases, our results show the function of N- and C-terminal domains of RdRp: the former opens the genome duplex to isolate the template strand; the latter splits the emerging template-transcript hybrid, guides genome reannealing to form a transcription bubble, and opens a capsid shell protein (CSP) to release the transcript. These two "helicase" domains also extensively interact with CSP, which has a switchable N-terminal helix that, like cellular transcriptional factors, either inhibits or promotes RdRp activity. The in situ structures of RdRp, CSP, and RNA in action inform mechanisms of not only transcription, but also replication.
External linksPubMed:31101900 / Publisher's page
KeywordsAnimals / Capsid Proteins / Cell Line / Cercopithecus aethiops / Cryoelectron Microscopy / DNA Replication / Models, Molecular / Protein Domains / RNA Replicase / RNA, Double-Stranded / RNA, Messenger / RNA, Viral / Rotavirus / Transcription, Genetic / Virus Replication / viral protein/transferase/rna / RNA-dependent RNA polymerase / capsid shell protein / transcription / in situ structure / rotavirus / transcriptional factors / reovirus / VIRUS / viral protein-transferase-rna complex / viral protein/rna/transferase / viral protein-rna-transferase complex
MethodsEM (single particle)
Resolution3.4 - 3.6 A
Structure data

EMDB-20059:
In situ structure of Rotavirus RNA-dependent RNA polymerase at duplex-open state

EMDB-20060:
In situ structure of Rotavirus RNA-dependent RNA polymerase at transcript-elongated state

PDB-6ogy:
In situ structure of Rotavirus RNA-dependent RNA polymerase at duplex-open state

PDB-6ogz:
In situ structure of Rotavirus RNA-dependent RNA polymerase at transcript-elongated state

Chemicals

ChemComp-UTP:
URIDINE 5'-TRIPHOSPHATEUridine triphosphate

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATEGuanosine triphosphate

Source
  • rotavirus a

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