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

SASDU47 – Non-homologous end-joining factor 1 - XLF

Non-homologous end-joining factor 1
MWexperimental 74 kDa
MWexpected 67 kDa
VPorod 123 nm3
log I(s) 7.45×10-2 7.45×10-3 7.45×10-4 7.45×10-5
Non-homologous end-joining factor 1 small angle scattering data  s, nm-1
ln I(s)
Non-homologous end-joining factor 1 Guinier plot ln 7.45×10-2 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Non-homologous end-joining factor 1 Kratky plot 1.104 0 √3 sRg
p(r)
Non-homologous end-joining factor 1 pair distance distribution function Rg: 3.6 nm 0 Dmax: 12.1 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of non-homologous end-joining factor 1 (XLF) 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 = 0.10331 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.85 mg/ml was measured at 20°C. 630 successive 0.610 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.

Non-homologous end-joining factor 1 (XLF)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   33.5 kDa
 
UniProt   Q9H9Q4 (1-299)
Sequence   FASTA