Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose) (original) (raw)
- Brief Communication
- Published: 24 January 2010
- Christoph Brockmann1 na1,
- Pawan Vinod Mehrotra2,
- Ji-Chun Yang1,
- David Loakes1,
- Stephen C West3,
- Ivan Ahel2 &
- …
- David Neuhaus1
Nature Structural & Molecular Biology volume 17, pages 241–243 (2010)Cite this article
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Abstract
Addition of poly(ADP-ribose) (PAR) is an important post-translational modification in higher eukaryotes. Several DNA repair and checkpoint proteins possess specific PAR-binding zinc-finger (PBZ) modules critical for function. Here, we present solution structures of the two PBZ modules of aprataxin and PNK–like factor (APLF), revealing a novel type of zinc finger. By combining in vivo PAR-binding data with NMR interaction data using PAR fragments, we propose a structural basis for PBZ-PAR recognition.
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Acknowledgements
We thank A. Murzin, A. Andreeva and C. Rademacher for helpful discussions, G. Smith (AstraZeneca) for the PARP inhibitor KU-0058948, W. Vranken for help with data deposition and C. Oubridge for help with MS. S.E. was funded by a studentship from Boehringer Ingelheim Fonds, C.B. by a fellowship from the Federation of European Biochemical Societies and I.A. by fellowships from Cancer Research UK and the Louis-Jeantet Foundation.
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- Sebastian Eustermann and Christoph Brockmann: These authors contributed equally to this work.
Authors and Affiliations
- MRC Laboratory of Molecular Biology, Cambridge, UK
Sebastian Eustermann, Christoph Brockmann, Ji-Chun Yang, David Loakes & David Neuhaus - Paterson Institute for Cancer Research, University of Manchester, Manchester, UK
Pawan Vinod Mehrotra & Ivan Ahel - Cancer Research UK, London Research Institute, Clare Hall Laboratories, Hertfordshire, South Mimms, UK
Stephen C West
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- Sebastian Eustermann
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Contributions
S.E. cloned the construct; S.E., P.V.M. and I.A. designed and performed biochemical experiments; D.L. synthesized the RFA ligand; P.V.M. performed the in vivo binding analyses; S.E., J.-C.Y. and C.B. performed and analyzed NMR experiments; S.E., C.B. and D.N. calculated and analyzed the structures; S.E., I.A., S.C.W. and D.N. wrote the manuscript; D.N. supervised the project.
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Correspondence toDavid Neuhaus.
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The authors declare no competing financial interests.
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Eustermann, S., Brockmann, C., Mehrotra, P. et al. Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose).Nat Struct Mol Biol 17, 241–243 (2010). https://doi.org/10.1038/nsmb.1747
- Received: 21 July 2009
- Accepted: 17 November 2009
- Published: 24 January 2010
- Issue Date: February 2010
- DOI: https://doi.org/10.1038/nsmb.1747