ジャーナル: Nat Commun / 年: 2024 タイトル: Structures of the mumps virus polymerase complex via cryo-electron microscopy. 著者: Tianhao Li / Mingdong Liu / Zhanxi Gu / Xin Su / Yunhui Liu / Jinzhong Lin / Yu Zhang / Qing-Tao Shen / 要旨: 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), ...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.
全体 : The MuV polymerase complex of RNA-directed RNA polymerase L with ...
全体
名称: The MuV polymerase complex of RNA-directed RNA polymerase L with tetrameric phosphoproteins
要素
複合体: The MuV polymerase complex of RNA-directed RNA polymerase L with tetrameric phosphoproteins
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超分子 #1: The MuV polymerase complex of RNA-directed RNA polymerase L with ...
超分子
名称: The MuV polymerase complex of RNA-directed RNA polymerase L with tetrameric phosphoproteins タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#2 詳細: The MuV polymerase complex expressed in Sf9 cells and purified by affinity chromatography and size-exlusive chromatography sequentially.