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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Ding K,Celma CC,Zhang X,Chang T,Shen W,Atanasov I,Roy P,Zhou ZHdoi
10.1038/s41467-019-10236-7subject
Has Abstractpub_date
2019-05-17 00:00:00pages
2216issue
1issn
2041-1723pii
10.1038/s41467-019-10236-7journal_volume
10pub_type
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