tetano
Editor, Senior Moderator
Mol Cell. 2015 Jan 21. pii: S1097-2765(14)01009-0. doi: 10.1016/j.molcel.2014.12.031. [Epub ahead of print]
[h=1]Cryo-EM Structure of Influenza Virus RNA Polymerase Complex at 4.3 ? Resolution.[/h] Chang S[SUP]1[/SUP], Sun D[SUP]1[/SUP], Liang H[SUP]1[/SUP], Wang J[SUP]2[/SUP], Li J[SUP]1[/SUP], Guo L[SUP]1[/SUP], Wang X[SUP]1[/SUP], Guan C[SUP]1[/SUP], Boruah BM[SUP]1[/SUP], Yuan L[SUP]1[/SUP], Feng F[SUP]1[/SUP], Yang M[SUP]1[/SUP], Wang L[SUP]3[/SUP], Wang Y[SUP]3[/SUP], Wojdyla J[SUP]4[/SUP], Li L[SUP]5[/SUP], Wang J[SUP]2[/SUP], Wang M[SUP]4[/SUP], Cheng G[SUP]3[/SUP], Wang HW[SUP]6[/SUP], Liu Y[SUP]7[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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 ?, 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.
Copyright ? 2015 Elsevier Inc. All rights reserved.
PMID: 25620561 [PubMed - as supplied by publisher]
[h=1]Cryo-EM Structure of Influenza Virus RNA Polymerase Complex at 4.3 ? Resolution.[/h] Chang S[SUP]1[/SUP], Sun D[SUP]1[/SUP], Liang H[SUP]1[/SUP], Wang J[SUP]2[/SUP], Li J[SUP]1[/SUP], Guo L[SUP]1[/SUP], Wang X[SUP]1[/SUP], Guan C[SUP]1[/SUP], Boruah BM[SUP]1[/SUP], Yuan L[SUP]1[/SUP], Feng F[SUP]1[/SUP], Yang M[SUP]1[/SUP], Wang L[SUP]3[/SUP], Wang Y[SUP]3[/SUP], Wojdyla J[SUP]4[/SUP], Li L[SUP]5[/SUP], Wang J[SUP]2[/SUP], Wang M[SUP]4[/SUP], Cheng G[SUP]3[/SUP], Wang HW[SUP]6[/SUP], Liu Y[SUP]7[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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 ?, 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.
Copyright ? 2015 Elsevier Inc. All rights reserved.
PMID: 25620561 [PubMed - as supplied by publisher]