Dimerization of ADAR1 modulates site-specificity of RNA editing

Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P, Nature Communications 15(1) (2024) DOI

SASDVL7 – Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2)

Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2)
MWexperimental 11 kDa
MWexpected 13 kDa
VPorod 16 nm3
log I(s) 1.12×10-2 1.12×10-3 1.12×10-4 1.12×10-5
Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) small angle scattering data  s, nm-1
ln I(s)
Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) Guinier plot ln 1.12×10-2 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) Kratky plot 1.104 0 3 sRg
p(r)
Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) pair distance distribution function Rg: 2.1 nm 0 Dmax: 6.4 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) in 20 mM Na-phosphate, 100 mM NaCl, 2 mM 2-mercaptoethanol, pH 7 were collected on the SWING beam line at the SOLEIL storage ring (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 10°C. 19 successive 0.990 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.

Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) (ADAR1-ds3/Xlrbpa-ds2)
Mol. type   Protein
Organism   Homo sapiens / Xenopus laevis
Olig. state   Monomer
Mon. MW   12.8 kDa
 
UniProt   P55265 (708-801)
Sequence   FASTA