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S. Reports and |. , For Influenza A and B viruses, several studies have shown that the nuclear localization signals (NLS) of NP recognized by the cellular importins-?, are located within the flexible N-terminal tail 17-24 . Recently, crystal structures of the two NLSs of A/NP bound to importin-? have been solved 25,26 . In this paper, we characterized D/NP and solved the X-ray structure of its tetramer. The C-terminal D/NP TAIL harbouring a classical bipartite nuclear localization signal (NLS) was not visible in the structure. We designed two C-terminal truncated mutants (D/NP-511 and D/NP-529) to study the interaction of D/NP with importin-?7. Our biochemical experiments demonstrate that D/NP TAIL is involved in the interaction with importins-? and immunofluorescence showed that the wild-type D/NP goes into the nucleus whereas the mutants stay in the expression plasmid and over-expressed in Escherichia coli as a C-terminal His-tagged recombinant protein, Influenza viruses transcribe and replicate in the nucleus of the infected cells and the NPs and the polymerase subunits need to interact with the nuclear transport system of the cell, vol.9, 2019.

, 300 mM NaCl and 5 mM ?-mercaptoethanol. (b) SEC-MALLS-RI analysis of D/NP. SEC was performed with a Superdex TM 200 increase 10/300 GL column equilibrated with 20 mM Tris-HCl pH 7.5, 150 mM NaCl and 5 mM ?-ME. The panel shows the theoretical Mw and the measured Mw. (c) and (e) Electron microscopy images of the elution peak of D/NP and D/NP-511. Samples show different oligomeric states although most oligomers are tetramers. The scale bar corresponds to 100 nm, Figure 1. Purification and characterized of Influenza D nucleoprotein. (a) Size exclusion chromatography profile of wild-type D/NP. The sample was loaded on a Hiload TM 16/600 S200 column equilibrated with the running buffer 20 mM Tris-HCl pH 7.5

S. Reports and |. , Several internal loops were missing and the C-terminal 50 residues were disordered. The oligomerization-loop of one protomer plugged into a cavity of its neighbour (Fig. 2c). The N-terminal part of the loop started with a strictly conserved glutamate residue (Gln-414) that interacted with the backbone of the strictly conserved consecutive aromatic residues 499 FFF 501 . The loop was then stabilized by several kind of contacts; mainly hydrophobic (by the side chain of the strictly conserved Phe-421 and Val-423) and of several aromatic residues lying in the pocket of the neighbouring monomer but also the salt bridge between an arginine from one monomer (Arg-425) interacting with a glutamate of the neighbour (Glu-352; Fig. 2c,d), y molecules and a fourth protomer was fitted manually after the analysis of the electron density, vol.9, 2019.

, The overall folds of A/NP, B/NP, ISA/NP and D/NP were very similar (Fig. 3a) with root-mean-square deviations (rmsd) between 1.6 Å (for 383 C? for the comparison A/NP with B/NP) and 2, Core structure of all nucleoproteins (NP CORE ) with tails (NP TAIL )

I. Including and . Np, NP and D/NP and finishing with three hydrophobic residues, anchored into the surface of the protein (Supplementary Fig. 1). Figure 3b shows the X-ray structures of A/NP, B/NP, D/NP and ISA/NP with a zoom on the C-terminal regions, where a superimposed patch made by three consecutive aromatic residues is found in Influenza NPs ( 487 YFF 489 for A/NP, 545 FFF 547 for B/NP and 499 FFF 501 for D/NP). A similar patch is also present in the ISA/NP model ( 580 GLF 582 ). The NP CORE contains the large and shallow positively charged surface which might bind RNA (Fig. 3c), without sequence specificity (see above) 12,13,36,37 . Twenty or 71 residues without any structure are found N-terminally before the cores of A/ and B/NP whereas for D/NP, the core starts with a very short version of an N-terminal tail (only 7 residues), which seems to be compensated by the presence of a carboxy-terminal NP TAIL of 51 residues (Supplementary Fig. 1). The length of the NP TAILs is variable and its location seems to be specific for each genus, NPs can be defined based on the X-ray structures with the NP CORE starting with the first

, As intrinsically disordered proteins are known to be eluted from gel filtration with an aberrant volume 38,39 , a SEC-MALLS-RI experiment (Fig. 4c) confirmed the monodispersity of the purified sample with a Mw of 8.2 kDa for D/NP TAIL (with the His-tag). A circular dichroism analysis confirmed that D/NP TAIL did not contain any significant stable secondary structure in solution (Fig. 4d), even in presence of TMAO, D/NP TAIL behaves as an intrinsically disordered protein. Based on the crystal structure and a disorder prediction (Fig. 4a)

, We also confirmed the interaction between the two partners using the full-length D/NP. Using surface plasmon resonance, we measured a Kd of 100 nM between immobilized D/NP TAIL and importin-?7 (Fig. 5c), ten-fold higher that the affinities measured for the N-terminally A/ and B/NP TAILs 18,25 . By gel filtration, we showed that the D/NP:importin-?7 complex could be eluted as a single peak. A molecular weight of 474 kDa has been measured by SEC-MALLS-RI for the complex (Fig. 5d), corresponding to the interaction of four molecules of importins-?7 (Mw = 4 × 55 kDa) per tetramer of D/NP (Mw = 260 kDa). To confirm the role of D/NP TAIL in the interaction with importin-?, D/NP TAIL interacts with importin-?. The N-terminal tails of A/NP and B/NP are known to be involved in the nuclear import by interacting with importins-?, p.43

S. Reports and |. , D/NP, D/NP-511 and D/NP-529 DNA coding sequences were cloned in pETM13 (EMBL) to express C-terminal His-tagged proteins whereas D/NP TAIL (505-D/NP-552) DNA coding sequence was cloned in pETM11 (EMBL) to express an N-terminal His-tagged fragment. The DNA coding sequence of the human importin-?7 (KPNA6; Uniprot accession number O60684) was cloned without its IBB domain (amino-acids 58 to 536) in pET9a (Novagen) to express an N-terminal His-tagged protein 63 . Sequencing was performed by Eurofins. Expression and purification of proteins. Escherichia coli BL21 RIL (DE3) cells (Life Technology) were transformed with the resulting plasmids. Cultures were induced 12 h by adding 0.3 mM isopropyl-?-Dthiogalactopyranoside (IPTG) at 18 °C and collected by centrifugation. The pellets were resuspended and sonicated in 50 mM Tris-HCl pH 7.5, 300 mM NaCl, 1 M NDSB-201 (Sigma), 2 mM ?-mercaptoethanol (?-ME) and complete protease inhibitor cocktail (Roche) for D/NP constructs and 50 mM Tris-HCl pH 8, 500 mM NaCl, 1 mM ?-ME and complete protease inhibitor cocktail for importin-?7. All purifications were performed at room temperature. All D/NP constructs were purified by nickel affinity chromatography (Ni-NTA, Qiagen) followed, y the C-terminal N TAIL . If we could generate Influenza RNPs with NP without NP TAIL to rigidify the RNPs, it would make it easier solving a high resolution structure to observe the RNA on the nucleoproteins, vol.9, 2019.

S. Reports and |. , determine the kinetic parameters were kept below 3, due to the obtained high signal, and T-value for rate parameters above at least 30. The residuals for the fitting were kept between 1 and ?1. Nuclear import of WT and NP mutants in HEK 293T cells. Plasmids. The D/NP, D/NP-511 and D/ NP-529 genes were amplified by PCR, cloned into the multiple cloning site of pSC-A-amp/kan vector (Strataclone blunt kit, Agilent) and expressed into competent bacterial cells, according to the manufacturer's instructions. The NP genes in pSC-A-amp/kan vector were cloned into KpnI and BamHI restriction sites of an eukaryotic expression vector, vol.9, 2019.

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