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

SASDVK7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant)

Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant)
MWexperimental 12 kDa
MWexpected 12 kDa
VPorod 20 nm3
log I(s) 1.01×10-2 1.01×10-3 1.01×10-4 1.01×10-5
Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) small angle scattering data  s, nm-1
ln I(s)
Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) Guinier plot ln 1.02×10-2 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) Kratky plot 1.104 0 √3 sRg
p(r)
Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) pair distance distribution function Rg: 2.2 nm 0 Dmax: 7.2 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) 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. 25 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.

Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) (Mutant-ADAR1-dsRBD3)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   12.5 kDa
 
UniProt   P55265 (708-801)
Sequence   FASTA