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TitleIn situ structures of polymerase complex of mammalian reovirus illuminate RdRp activation and transcription regulation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 119, Issue 50, Page e2203054119, Year 2022
Publish dateDec 13, 2022
AuthorsKeyan Bao / Xueli Zhang / Dongyu Li / Wei Sun / Zhenzhao Sun / Jingfei Wang / Ping Zhu /
PubMed AbstractMammalian reovirus (reovirus) is a multilayered, turreted member of characterized by transcription of dsRNA genome within the innermost capsid shell. Here, we present high-resolution in situ ...Mammalian reovirus (reovirus) is a multilayered, turreted member of characterized by transcription of dsRNA genome within the innermost capsid shell. Here, we present high-resolution in situ structures of reovirus transcriptase complex in an intact double-layered virion, and in the uncoated single-layered core particles in the unloaded, reloaded, pre-elongation, and elongation states, respectively, obtained by cryo-electron microscopy and sub-particle reconstructions. At the template entry of RNA-dependent RNA polymerase (RdRp), the RNA-loading region gets flexible after uncoating resulting in the unloading of terminal genomic RNA and inactivity of transcription. However, upon adding transcriptional substrates, the RNA-loading region is recovered leading the RNAs loaded again. The priming loop in RdRp was found to play a critical role in regulating transcription, which hinders the elongation of transcript in virion and triggers the rearrangement of RdRp C-terminal domain (CTD) during elongation, resulting in splitting of template-transcript hybrid and opening of transcript exit. With the integration of these structures, a transcriptional model of reovirus with five states is proposed. Our structures illuminate the RdRp activation and regulation of the multilayered turreted reovirus.
External linksProc Natl Acad Sci U S A / PubMed:36469786 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 3.6 Å
Structure data

33770

7yed

EMDB-33770, PDB-7yed:
In situ structure of polymerase complex of mammalian reovirus in the elongation state
Method: EM (single particle) / Resolution: 3.0 Å

33778

7yev

EMDB-33778, PDB-7yev:
In situ structure of polymerase complex of mammalian reovirus in the pre-elongation state
Method: EM (single particle) / Resolution: 3.6 Å

33779

7yez

EMDB-33779, PDB-7yez:
In situ structure of polymerase complex of mammalian reovirus in the reloaded state
Method: EM (single particle) / Resolution: 3.4 Å

33780

7yf0

EMDB-33780, PDB-7yf0:
In situ structure of polymerase complex of mammalian reovirus in the core
Method: EM (single particle) / Resolution: 3.4 Å

33787

7yfe

EMDB-33787, PDB-7yfe:
In situ structure of polymerase complex of mammalian reovirus in virion
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SAM:
S-ADENOSYLMETHIONINE / S-Adenosyl methionine

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

ChemComp-UTP:
URIDINE 5'-TRIPHOSPHATE / UTP*YM / Uridine triphosphate

ChemComp-MG:
Unknown entry

Source
  • mammalian orthoreovirus 3
KeywordsVIRAL PROTEIN/RNA / mammalian reovirus / cryo-em / RNA dependent RNA polymerase / transcription / VIRAL PROTEIN / VIRAL PROTEIN-RNA complex

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