A prion-like domain is required for phase separation and chloroplast RNA processing during cold acclimation in Arabidopsis.

Legen J, Lenzen B, Kachariya N Feltgen S, Gao Y, Mergenthal S, Weber W, Klotzsch E, Zoschke R, Sattler M, Schmitz-Linneweber C, Plant Cell (2024) Europe PMC

SASDT92 – Prion-like domain of 29 kDa chloroplastic ribonucleoprotein measured at at 298 K from Arabidopsis thaliana (Mouse-ear cress)

29 kDa ribonucleoprotein, chloroplastic
MWexperimental 8 kDa
MWexpected 8 kDa
VPorod 19 nm3
log I(s) 4.64×10-1 4.64×10-2 4.64×10-3 4.64×10-4
29 kDa ribonucleoprotein, chloroplastic small angle scattering data  s, nm-1
ln I(s)
29 kDa ribonucleoprotein, chloroplastic Guinier plot ln 4.64×10-1 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
29 kDa ribonucleoprotein, chloroplastic Kratky plot 1.104 0 3 sRg
p(r)
29 kDa ribonucleoprotein, chloroplastic pair distance distribution function Rg: 2.3 nm 0 Dmax: 9.2 nm

Data validation


There are no models related to this curve.

SAXS data from solutions of the prion-like domain from 29 kDa chloroplastic ribonucleoprotein in 20 mM sodium phosphate, 30 mM NaCl, pH 6.2 were collected using a Rigaku BioSAXS-1000 instrument (Technische Universität München, Garching, Germany) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.155 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.00 mg/ml was measured at 25°C. Eight successive 900 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.

29 kDa ribonucleoprotein, chloroplastic (PLD of CP29A)
Mol. type   Protein
Organism   Arabidopsis thaliana
Olig. state   Monomer
Mon. MW   7.7 kDa
 
UniProt   Q43349 (176-254)
Sequence   FASTA