Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro.

Vu DD, Bonucci A, Brenière M, Cisneros-Aguirre M, Pelupessy P, Wang Z, Carlier L, Bouvignies G, Cortes P, Aggarwal AK, Blackledge M, Gueroui Z, Belle V, Stark JM, Modesti M, Ferrage F, Nat Struct Mol Biol (2024) Europe PMC

SASDU57 – DNA repair protein XRCC4 in complex with BRCT domains of DNA ligase 4

DNA repair protein XRCC4
DNA ligase 4
MWexperimental 147 kDa
MWexpected 108 kDa
VPorod 248 nm3
log I(s) 2.11×10-1 2.11×10-2 2.11×10-3 2.11×10-4
DNA repair protein XRCC4 DNA ligase 4 small angle scattering data  s, nm-1
ln I(s)
DNA repair protein XRCC4 DNA ligase 4 Guinier plot ln 2.12×10-1 Rg: 5.8 nm 0 (5.8 nm)-2 s2
(sRg)2I(s)/I(0)
DNA repair protein XRCC4 DNA ligase 4 Kratky plot 1.104 0 √3 sRg
p(r)
DNA repair protein XRCC4 DNA ligase 4 pair distance distribution function Rg: 6.1 nm 0 Dmax: 23.0 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of DNA repair protein XRCC4 in complex with BRCT domains of DNA ligase 4 in 20 mM Bis-tris, 150 mM KCl, 1 mM EDTA, 1 mM DTT, pH 6.5 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 = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 9.90 mg/ml was measured at 20°C. 630 successive 0.619 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.

DNA repair protein XRCC4 (XRCC4)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   38.4 kDa
 
UniProt   Q13426 (1-336)
Sequence   FASTA
 
DNA ligase 4 (LIG4)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   30.9 kDa
 
UniProt   P49917 (643-911)
Sequence   FASTA