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Biomolecules 2013, 3(1), 1-17; doi:10.3390/biom3010001
Review

Molecular Insights into Poly(ADP-ribose) Recognition and Processing

1,2
,
2
,
1
 and
1,*
1 Cancer Research UK, Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK 2 Rudjer Boskovic Institute, Bijenicka 54, Zagreb 10000, Croatia
* Author to whom correspondence should be addressed.
Received: 24 October 2012 / Revised: 1 December 2012 / Accepted: 17 December 2012 / Published: 21 December 2012
(This article belongs to the Special Issue DNA Damage Response)
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Abstract

Poly(ADP-ribosyl)ation is a post-translational protein modification involved in the regulation of important cellular functions including DNA repair, transcription, mitosis and apoptosis. The amount of poly(ADP-ribosyl)ation (PAR) in cells reflects the balance of synthesis, mediated by the PARP protein family, and degradation, which is catalyzed by a glycohydrolase, PARG. Many of the proteins mediating PAR metabolism possess specialised high affinity PAR-binding modules that allow the efficient sensing or processing of the PAR signal. The identification of four such PAR-binding modules and the characterization of a number of proteins utilising these elements during the last decade has provided important insights into how PAR regulates different cellular activities. The macrodomain represents a unique PAR-binding module which is, in some instances, known to possess enzymatic activity on ADP-ribose derivatives (in addition to PAR-binding). The most recently discovered example for this is the PARG protein, and several available PARG structures have provided an understanding into how the PARG macrodomain evolved into a major enzyme that maintains PAR homeostasis in living cells.
Keywords: Poly(ADP-ribose); PARP; PARG; macrodomain; protein modification Poly(ADP-ribose); PARP; PARG; macrodomain; protein modification
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Žaja, R.; Mikoč, A.; Barkauskaite, E.; Ahel, I. Molecular Insights into Poly(ADP-ribose) Recognition and Processing. Biomolecules 2013, 3, 1-17.

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