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In situ structures of rotavirus polymerase in action and mechanism of mRNA transcription and release

Author

Listed:
  • Ke Ding

    (University of California
    University of California
    University of California)

  • Cristina C. Celma

    (London School of Hygiene and Tropical Medicine)

  • Xing Zhang

    (University of California)

  • Thomas Chang

    (University of California
    University of California)

  • Wesley Shen

    (University of California
    University of California)

  • Ivo Atanasov

    (University of California)

  • Polly Roy

    (London School of Hygiene and Tropical Medicine)

  • Z. Hong Zhou

    (University of California
    University of California
    University of California)

Abstract

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.

Suggested Citation

  • Ke Ding & Cristina C. Celma & Xing Zhang & Thomas Chang & Wesley Shen & Ivo Atanasov & Polly Roy & Z. Hong Zhou, 2019. "In situ structures of rotavirus polymerase in action and mechanism of mRNA transcription and release," Nature Communications, Nature, vol. 10(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10236-7
    DOI: 10.1038/s41467-019-10236-7
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    Cited by:

    1. Zhiqiang Li & Han Xia & Guibo Rao & Yan Fu & Tingting Chong & Kexing Tian & Zhiming Yuan & Sheng Cao, 2024. "Cryo-EM structures of Banna virus in multiple states reveal stepwise detachment of viral spikes," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. Simon Jenni & Joshua A. Horwitz & Louis-Marie Bloyet & Sean P. J. Whelan & Stephen C. Harrison, 2022. "Visualizing molecular interactions that determine assembly of a bullet-shaped vesicular stomatitis virus particle," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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