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Publication Abstract from PubMed

The viral polymerase complex, comprising the large protein (L) and phosphoprotein (P), is crucial for both genome replication and transcription in non-segmented negative-strand RNA viruses (nsNSVs), while structures corresponding to these activities remain obscure. Here, we resolved two L-P complex conformations from the mumps virus (MuV), a typical member of nsNSVs, via cryogenic-electron microscopy. One conformation presents all five domains of L forming a continuous RNA tunnel to the methyltransferase domain (MTase), preferably as a transcription state. The other conformation has the appendage averaged out, which is inaccessible to MTase. In both conformations, parallel P tetramers are revealed around MuV L, which, together with structures of other nsNSVs, demonstrates the diverse origins of the L-binding X domain of P. Our study links varying structures of nsNSV polymerase complexes with genome replication and transcription and points to a sliding model for polymerase complexes to advance along the RNA templates.

Structures of the mumps virus polymerase complex via cryo-electron microscopy.,Li T, Liu M, Gu Z, Su X, Liu Y, Lin J, Zhang Y, Shen QT Nat Commun. 2024 May 17;15(1):4189. doi: 10.1038/s41467-024-48389-9. PMID:38760379^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.