La protein binding to telomerase RNA supports an evolutionary relationship between plant and ciliate telomerase pathways.

Jenner L, Pruchkouski D, Štefanovie B, Nováková O, Kubíčková M, Fajkus P, Brázdová M, Paleček J, Sýkorová E, Nucleic Acids Res 54(5) (2026) Europe PMC

SASDYQ2 – C-terminal domain of La protein 1

C-terminal domain of La protein 1
MWexperimental 12 kDa
MWexpected 22 kDa
VPorod 24 nm3
log I(s) 2.78×10-1 2.78×10-2 2.78×10-3 2.78×10-4
C-terminal domain of La protein 1 small angle scattering data  s, nm-1
ln I(s)
C-terminal domain of La protein 1 Guinier plot ln 2.78×10-1 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
C-terminal domain of La protein 1 Kratky plot 1.104 0 √3 sRg
p(r)
C-terminal domain of La protein 1 pair distance distribution function Rg: 2.9 nm 0 Dmax: 10.7 nm

Data validation

Fits and models

log I(s)
 s, nm-1
C-terminal domain of La protein 1 Rg histogram Rg, nm
C-terminal domain of La protein 1 EOM/RANCH model
C-terminal domain of La protein 1 EOM/RANCH model
C-terminal domain of La protein 1 EOM/RANCH model
SAXS data from solutions of C-terminal domain of La protein 1 in 100 mM Tris-HCl, 500 mM NaCl, pH 8 were collected on the Rigaku BioSAXS-2000 instrument (CEITEC, Brno, Czech Republic) using a Rigaku HyPix-3000 detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 1.54 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 20°C. 12 successive 300 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.

C-terminal domain of La protein 1
Mol. type   Protein
Organism   Arabidopsis thaliana
Olig. state   Monomer
Mon. MW   22.1 kDa
 
UniProt   Q93ZV7-1 (236-433)
Sequence   FASTA