Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	The host RNA polymerase II C-terminal domain is the anchor for replication of the influenza virus genome.
Journal, issue, pages	Nat Commun, Vol. 15, Issue 1, Page 1064, Year 2024
Publish date	Feb 5, 2024
Authors	Tim Krischuns / Benoît Arragain / Catherine Isel / Sylvain Paisant / Matthias Budt / Thorsten Wolff / Stephen Cusack / Nadia Naffakh /
PubMed Abstract	The current model is that the influenza virus polymerase (FluPol) binds either to host RNA polymerase II (RNAP II) or to the acidic nuclear phosphoprotein 32 (ANP32), which drives its conformation ...The current model is that the influenza virus polymerase (FluPol) binds either to host RNA polymerase II (RNAP II) or to the acidic nuclear phosphoprotein 32 (ANP32), which drives its conformation and activity towards transcription or replication of the viral genome, respectively. Here, we provide evidence that the FluPol-RNAP II binding interface, beyond its well-acknowledged function in cap-snatching during transcription initiation, has also a pivotal role in replication of the viral genome. Using a combination of cell-based and in vitro approaches, we show that the RNAP II C-terminal-domain, jointly with ANP32, enhances FluPol replication activity. We observe successive conformational changes to switch from a transcriptase to a replicase conformation in the presence of the bound RNPAII C-terminal domain and propose a model in which the host RNAP II is the anchor for transcription and replication of the viral genome. Our data open new perspectives on the spatial coupling of viral transcription and replication and the coordinated balance between these two activities.
External links	Nat Commun / PubMed:38316757 / PubMed Central
Methods	EM (single particle)
Resolution	2.49 - 3.43 Å
Structure data	17755 8pm0 EMDB-17755, PDB-8pm0: Influenza A/H7N9 polymerase in replicase-like conformation in pre-initiation state with Pol II pS5 CTD peptide mimic bound in site 1A/2A Method: EM (single particle) / Resolution: 2.9 Å 17782 8pnp EMDB-17782, PDB-8pnp: Influenza A/H7N9 polymerase in pre-initiation state with continuous Pol II pS5 CTD peptide mimic bound in site 1A/2A Method: EM (single particle) / Resolution: 2.49 Å 17783 8pnq EMDB-17783, PDB-8pnq: Influenza A/H7N9 polymerase in elongation state with continuous Pol II pS5 CTD peptide mimic bound in site 1A/2A Method: EM (single particle) / Resolution: 2.88 Å 17792 8poh EMDB-17792, PDB-8poh: Influenza A/H7N9 polymerase symmetric dimer bound to the promoter (PA K289A/C489R) Method: EM (single particle) / Resolution: 3.3 Å 18871 8r3k EMDB-18871, PDB-8r3k: Influenza A/H7N9 polymerase in self-stalled pre-termination state, with Pol II pS5 CTD peptide mimic bound in site 1A/2A. Method: EM (single particle) / Resolution: 3.43 Å 18872 8r3l EMDB-18872, PDB-8r3l: Influenza A/H7N9 polymerase in pre-initiation state, intermediate conformation (I) with PB2-C(I), ENDO(T), and Pol II pS5 CTD peptide mimic bound in site 1A/2A Method: EM (single particle) / Resolution: 3.25 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-HOH: WATER / Water ChemComp-2KH: 5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]uridine ChemComp-POP: PYROPHOSPHATE 2- / Pyrophosphate
Source	influenza a virus (a/zhejiang/dtid-zju01/2013(h7n9)) homo sapiens (human)
Keywords	VIRAL PROTEIN / Viral polymerase