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 Jun 19)

PMID: 38898102 doi: 10.1038/s41594-024-01339-x

Submitted to SASBDB: 2024 Apr 9 Published in SASBDB: 2024 May 25

SASDU47 – Non-homologous end-joining factor 1 - XLF Sample: Non-homologous end-joining factor 1 dimer, 67 kDa Homo sapiens protein Buffer: 20 mM Bis-tris, 150 mM KCl, 1 mM EDTA, 1 mM DTT, pH: 6.5 Experiment: SAXS data collected at SWING, SOLEIL on 2021 Mar 13 RgGuinier 3.6 nm Dmax 12.1 nm VolumePorod 123 nm3

SASDU57 – DNA repair protein XRCC4 in complex with BRCT domains of DNA ligase 4 Sample: DNA repair protein XRCC4 dimer, 77 kDa Homo sapiens protein DNA ligase 4 monomer, 31 kDa Homo sapiens protein Buffer: 20 mM Bis-tris, 150 mM KCl, 1 mM EDTA, 1 mM DTT, pH: 6.5 Experiment: SAXS data collected at SWING, SOLEIL on 2021 Mar 13 RgGuinier 5.8 nm Dmax 23.0 nm VolumePorod 248 nm3

SASDU67 – The C-terminal region of DNA repair protein XRCC4 Sample: DNA repair protein XRCC4 monomer, 15 kDa Homo sapiens protein Buffer: 20 mM Bis-tris, 150 mM KCl, 1 mM EDTA, 1 mM DTT, pH: 6.5 Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Oct 20 RgGuinier 3.4 nm Dmax 11.1 nm VolumePorod 41 nm3