Acknowledgments
J.B.C. is supported by ARC program (SLS220120605310), ANR
(ANR-12-SVSE8-012), INCA DomRep (PLBIO 2012-280), and
CEFIPRA grant 5203C and by the French Infrastructure for
Integrated Structural Biology (FRISBI) (ANR-10-INBS-05).
A.G. is supported by a CIFRE PhD fellowship with Sanofi. We
thank Pierre Soule from Nanotemper Technologies for his availability and all the fruitful discussion. The experiments were performed on the Platform PIM (Platform for measurements of
Interactions of Macromolecules) (https://www.i2bc.paris-saclay.
fr/spip.php?article280).
References
1. Gavin AC, Bosche M, Krause R et al (2002)
Functional organization of the yeast proteome
by systematic analysis of protein complexes.
Nature 415(6868):141–147
2. Uetz P, Giot L, Cagney G et al (2000) A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403
(6770):623–627
3. Walker JR, Corpina RA, Goldberg J (2001)
Structure of the Ku heterodimer bound to
DNA and its implications for double-strand
break repair. Nature 412(6847):607–614
4. Blier PR, Griffith AJ, Craft J, Hardin JA (1993)
Binding of Ku protein to DNA. Measurement
of affinity for ends and demonstration of binding to nicks. J Biol Chem 268(10):7594–7601
5. Arosio D, Costantini S, Kong Y, Vindigni A
(2004) Fluorescence anisotropy studies on the
Ku-DNA interaction: anion and cation effects.
J Biol Chem 279(41):42826–42835
6. Tadi SK, Tellier-Lebegue C, Nemoz C et al
(2016) PAXX is an accessory c-NHEJ factor
that associates with Ku70 and has overlapping
functions with XLF. Cell Rep 17(2):541–555
7. Britton S, Coates J, Jackson SP (2013) A new
method for high-resolution imaging of Ku foci
to decipher mechanisms of DNA doublestrand break repair. J Cell Biol 202
(3):579–595
8. Chang HHY, Pannunzio NR, Adachi N, Lieber MR (2017) Non-homologous DNA end
joining and alternative pathways to doublestrand break repair. Nat Rev Mol Cell Biol 18
(8):495–506
9. Frit P, Ropars V, Modesti M, Charbonnier JB,
Calsou P (2019) Plugged into the Ku-DNA
hub: the NHEJ network. Prog Biophys Mol
Biol 147:62–76
10. Nemoz C, Ropars V, Frit P et al (2018) XLF
and APLF bind Ku80 at two remote sites to
ensure DNA repair by non-homologous end
joining. Nat Struct Mol Biol 25(10):971–980
11. Ropars V, Drevet P, Legrand P et al (2011)
Structural characterization of filaments formed
by human Xrcc4-Cernunnos/XLF complex
involved
in
nonhomologous
DNA
end-joining. Proc Natl Acad Sci U S A 108
(31):12663–12668
12. Malivert L, Ropars V, Nunez M et al (2010)
Delineation of the Xrcc4-interacting region in
the globular head domain of cernunnos/XLF.
J Biol Chem 285(34):26475–26483
13. Bacquin A, Pouvelle C, Siaud N et al (2013)
The helicase FBH1 is tightly regulated by
PCNA via CRL4(Cdt2)-mediated proteolysis
in human cells. Nucleic Acids Res 41
(13):6501–6513
14. Dherin C, Gueneau E, Francin M et al (2009)
Characterization of a highly conserved binding
site of Mlh1 required for exonuclease
I-dependent mismatch repair. Mol Cell Biol
29(3):907–918
15. Liberti SE, Andersen SD, Wang J et al (2011)
Bi-directional routing of DNA mismatch repair
protein human exonuclease 1 to replication
foci and DNA double strand breaks. DNA
Repair (Amst) 10(1):73–86
16. Holdgate GA (2001) Making cool drugs hot:
isothermal titration calorimetry as a tool to
study binding energetics. BioTechniques 31
(1):164–170
17. Krell T (2008) Microcalorimetry: a response to
challenges in modern biotechnology. Microb
Biotechnol 1(2):126–136
18. Velazquez-Campoy A, Freire E (2006) Isothermal titration calorimetry to determine
142
Amandine Gontier et al.
J.B.C. is supported by ARC program (SLS220120605310), ANR
(ANR-12-SVSE8-012), INCA DomRep (PLBIO 2012-280), and
CEFIPRA grant 5203C and by the French Infrastructure for
Integrated Structural Biology (FRISBI) (ANR-10-INBS-05).
A.G. is supported by a CIFRE PhD fellowship with Sanofi. We
thank Pierre Soule from Nanotemper Technologies for his availability and all the fruitful discussion. The experiments were performed on the Platform PIM (Platform for measurements of
Interactions of Macromolecules) (https://www.i2bc.paris-saclay.
fr/spip.php?article280).
References
1. Gavin AC, Bosche M, Krause R et al (2002)
Functional organization of the yeast proteome
by systematic analysis of protein complexes.
Nature 415(6868):141–147
2. Uetz P, Giot L, Cagney G et al (2000) A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403
(6770):623–627
3. Walker JR, Corpina RA, Goldberg J (2001)
Structure of the Ku heterodimer bound to
DNA and its implications for double-strand
break repair. Nature 412(6847):607–614
4. Blier PR, Griffith AJ, Craft J, Hardin JA (1993)
Binding of Ku protein to DNA. Measurement
of affinity for ends and demonstration of binding to nicks. J Biol Chem 268(10):7594–7601
5. Arosio D, Costantini S, Kong Y, Vindigni A
(2004) Fluorescence anisotropy studies on the
Ku-DNA interaction: anion and cation effects.
J Biol Chem 279(41):42826–42835
6. Tadi SK, Tellier-Lebegue C, Nemoz C et al
(2016) PAXX is an accessory c-NHEJ factor
that associates with Ku70 and has overlapping
functions with XLF. Cell Rep 17(2):541–555
7. Britton S, Coates J, Jackson SP (2013) A new
method for high-resolution imaging of Ku foci
to decipher mechanisms of DNA doublestrand break repair. J Cell Biol 202
(3):579–595
8. Chang HHY, Pannunzio NR, Adachi N, Lieber MR (2017) Non-homologous DNA end
joining and alternative pathways to doublestrand break repair. Nat Rev Mol Cell Biol 18
(8):495–506
9. Frit P, Ropars V, Modesti M, Charbonnier JB,
Calsou P (2019) Plugged into the Ku-DNA
hub: the NHEJ network. Prog Biophys Mol
Biol 147:62–76
10. Nemoz C, Ropars V, Frit P et al (2018) XLF
and APLF bind Ku80 at two remote sites to
ensure DNA repair by non-homologous end
joining. Nat Struct Mol Biol 25(10):971–980
11. Ropars V, Drevet P, Legrand P et al (2011)
Structural characterization of filaments formed
by human Xrcc4-Cernunnos/XLF complex
involved
in
nonhomologous
DNA
end-joining. Proc Natl Acad Sci U S A 108
(31):12663–12668
12. Malivert L, Ropars V, Nunez M et al (2010)
Delineation of the Xrcc4-interacting region in
the globular head domain of cernunnos/XLF.
J Biol Chem 285(34):26475–26483
13. Bacquin A, Pouvelle C, Siaud N et al (2013)
The helicase FBH1 is tightly regulated by
PCNA via CRL4(Cdt2)-mediated proteolysis
in human cells. Nucleic Acids Res 41
(13):6501–6513
14. Dherin C, Gueneau E, Francin M et al (2009)
Characterization of a highly conserved binding
site of Mlh1 required for exonuclease
I-dependent mismatch repair. Mol Cell Biol
29(3):907–918
15. Liberti SE, Andersen SD, Wang J et al (2011)
Bi-directional routing of DNA mismatch repair
protein human exonuclease 1 to replication
foci and DNA double strand breaks. DNA
Repair (Amst) 10(1):73–86
16. Holdgate GA (2001) Making cool drugs hot:
isothermal titration calorimetry as a tool to
study binding energetics. BioTechniques 31
(1):164–170
17. Krell T (2008) Microcalorimetry: a response to
challenges in modern biotechnology. Microb
Biotechnol 1(2):126–136
18. Velazquez-Campoy A, Freire E (2006) Isothermal titration calorimetry to determine
142
Amandine Gontier et al.