The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins

Gabrielle J. Grundy, Stuart L. Rulten, Raquel Arribas-Bosacoma, Kathryn Davidson, Zuzanna Kozik, Antony W. Oliver, Laurence H. Pearl and Keith W. Caldecott ()
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Gabrielle J. Grundy: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Stuart L. Rulten: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Raquel Arribas-Bosacoma: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Kathryn Davidson: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Zuzanna Kozik: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Antony W. Oliver: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Laurence H. Pearl: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex
Keith W. Caldecott: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex

Nature Communications, 2016, vol. 7, issue 1, 1-11

Abstract: Abstract The Ku-binding motif (KBM) is a short peptide module first identified in APLF that we now show is also present in Werner syndrome protein (WRN) and in Modulator of retrovirus infection homologue (MRI). We also identify a related but functionally distinct motif in XLF, WRN, MRI and PAXX, which we denote the XLF-like motif. We show that WRN possesses two KBMs; one at the N terminus next to the exonuclease domain and one at the C terminus next to an XLF-like motif. We reveal that the WRN C-terminal KBM and XLF-like motif function cooperatively to bind Ku complexes and that the N-terminal KBM mediates Ku-dependent stimulation of WRN exonuclease activity. We also show that WRN accelerates DSB repair by a mechanism requiring both KBMs, demonstrating the importance of WRN interaction with Ku. These data define a conserved family of KBMs that function as molecular tethers to recruit and/or stimulate enzymes during NHEJ.

Date: 2016
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DOI: 10.1038/ncomms11242

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