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• W2888681388 abstract "Nonhomologous end joining (NHEJ) is the primary pathway of DNA double-strand-break repair in vertebrate cells, yet how NHEJ factors assemble a synaptic complex that bridges DNA ends remains unclear. To address the role of XRCC4-like factor (XLF) in synaptic-complex assembly, we used single-molecule fluorescence imaging in Xenopus laevis egg extract, a system that efficiently joins DNA ends. We found that a single XLF dimer binds DNA substrates just before the formation of a ligation-competent synaptic complex between DNA ends. The interaction of both globular head domains of the XLF dimer with XRCC4 is required for efficient formation of this synaptic complex. Our results indicate that, in contrast to a model in which filaments of XLF and XRCC4 bridge DNA ends, binding of a single XLF dimer facilitates the assembly of a stoichiometrically well-defined synaptic complex. Single-molecule imaging of nonhomologous end joining in Xenopus egg extract reveals that a single XLF dimer aligns broken DNA ends for ligation." @default.
• W2888681388 created "2018-08-31" @default.
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• W2888681388 date "2018-09-01" @default.
• W2888681388 modified "2023-10-17" @default.
• W2888681388 title "A single XLF dimer bridges DNA ends during nonhomologous end joining" @default.
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• W2888681388 doi "https://doi.org/10.1038/s41594-018-0120-y" @default.
• W2888681388 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6128732" @default.
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