Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing.

Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T, Viruses 14(11) (2022) Europe PMC

SASDQR5 – Oligomerisation domain of phosphoprotein from Munia bornavirus

Phosphoprotein oligomerisation domain
MWexperimental 42 kDa
MWexpected 50 kDa
VPorod 70 nm3
log I(s) 3.23×10-2 3.23×10-3 3.23×10-4 3.23×10-5
Phosphoprotein oligomerisation domain small angle scattering data  s, nm-1
ln I(s)
Phosphoprotein oligomerisation domain Guinier plot ln 3.23×10-2 Rg: 4.6 nm 0 (4.6 nm)-2 s2
(sRg)2I(s)/I(0)
Phosphoprotein oligomerisation domain Kratky plot 1.104 0 √3 sRg
p(r)
Phosphoprotein oligomerisation domain pair distance distribution function Rg: 4.9 nm 0 Dmax: 17.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Phosphoprotein oligomerisation domain DAMMIF model
Synchrotron SAXS data from solutions of the oligomerisation domain of phosphoprotein from Munia bornavirus in 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH 7.5 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 8.00 μl sample at 12.4 mg/ml was injected at a 0.30 ml/min flow rate onto a column at 20°C. 540 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. SEC column = UNKNOWN

SEC column = UNKNOWN

Phosphoprotein oligomerisation domain (MuBV-1 POD)
Mol. type   Protein
Olig. state   Tetramer
Mon. MW   12.4 kDa
Sequence   FASTA