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PARP: a transferase by any other name

Nature Structural & Molecular Biology volume 15, pages 1243–1244 (2008)Cite this article

A recent report shows that several 'poly-ADP-ribose-polymerases' may function exclusively as a family of endogenous mono-ADP-ribosyltransferases, providing a new, molecularly less complex and broadened cellular role for this elusive post-translational modification.

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Figure 1: Domain architecture of the classic poly-ADP-ribose-polymerase PARP1 and the newly characterized mono-ADP-ribosyltransferase PARP10.
Figure 2: Classification of the poly-ADP-ribose-polymerase (PARP) family according to the structural model proposed by Kleine et al.7.

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Acknowledgements

K.D. is funded by the European Union FP6 Marie Curie Research and Training Network “Chromatin Plasticity”. S.T. and K.D. are students in the European Molecular Biology Laboratory's International PhD Programme. A.G.L. acknowledges the financial support of the European Molecular Biology Laboratory.

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  1. Susanne Till, Konstantina Diamantara and Andreas G. Ladurner are in the Gene Expression Unit and Structural & Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany. ladurner@embl.de,

    Susanne Till, Konstantina Diamantara & Andreas G Ladurner

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Till, S., Diamantara, K. & Ladurner, A. PARP: a transferase by any other name. Nat Struct Mol Biol 15, 1243–1244 (2008). https://doi.org/10.1038/nsmb1208-1243

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