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-Structure paper
タイトル | Cryo-EM structure of influenza virus RNA polymerase complex at 4.3 Å resolution. |
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ジャーナル・号・ページ | Mol Cell, Vol. 57, Issue 5, Page 925-935, Year 2015 |
掲載日 | 2015年3月5日 |
![]() | Shenghai Chang / Dapeng Sun / Huanhuan Liang / Jia Wang / Jun Li / Lu Guo / Xiangli Wang / Chengcheng Guan / Bhargavi M Boruah / Lingmin Yuan / Feng Feng / Mingrui Yang / Lulan Wang / Yao Wang / Justyna Wojdyla / Lanjuan Li / Jiawei Wang / Meitian Wang / Genhong Cheng / Hong-Wei Wang / Yingfang Liu / ![]() ![]() |
PubMed 要旨 | Replication and transcription of influenza virus genome mainly depend on its RNA-dependent RNA polymerase (RdRP), composed of the PA, PB1, and PB2 subunits. Although extensively studied, the ...Replication and transcription of influenza virus genome mainly depend on its RNA-dependent RNA polymerase (RdRP), composed of the PA, PB1, and PB2 subunits. Although extensively studied, the underlying mechanism of the RdRP complex is still unclear. Here we report the biochemical characterization of influenza RdRP subcomplex comprising PA, PB1, and N terminus of PB2, which exist as dimer in solution and can assemble into a tetramer state, regulated by vRNA promoter. Using single-particle cryo-electron microscopy, we have reconstructed the RdRP tetramer complex at 4.3 Å, highlighting the assembly and interfaces between monomers within the tetrameric structure. The individual RdRP subcomplex contains all the characterized motifs and appears as a cage-like structure. High-throughput mutagenesis profiling revealed that residues involved in the oligomer state formation are critical for viral life cycle. Our results lay a solid base for understanding the mechanism of replication of influenza and other negative-stranded RNA viruses. |
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手法 | EM (単粒子) |
解像度 | 4.3 - 6.8 Å |
構造データ | ![]() EMDB-6203: |
由来 |
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![]() | RNA BINDING PROTEIN/TRANSFERASE/RNA / Influenza RdRP / single particle reconstitution / replication / RNA BINDING PROTEIN-TRANSFERASE-RNA complex |