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

Ke Ding, Cristina C. Celma, Xing Zhang, Thomas Chang, Wesley Shen, Ivo Atanasov, Polly Roy () and Z. Hong Zhou ()
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Ke Ding: University of California
Cristina C. Celma: London School of Hygiene and Tropical Medicine
Xing Zhang: University of California
Thomas Chang: University of California
Wesley Shen: University of California
Ivo Atanasov: University of California
Polly Roy: London School of Hygiene and Tropical Medicine
Z. Hong Zhou: University of California

Nature Communications, 2019, vol. 10, issue 1, 1-9

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-10236-7

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