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Elsevier, Journal of Biological Chemistry, 11(285), p. 8054-8060, 2010

DOI: 10.1074/jbc.m109.077834

Elsevier, Journal of Biological Chemistry, 41(287), p. 34494, 2012

DOI: 10.1074/jbc.a109.077834

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PARP-3 Is a Mono-ADP-ribosylase That Activates PARP-1 in the Absence of DNA*

Journal article published in 2010 by Olga Loseva, Ann-Sofie Jemth, Helen E. Bryant, Herwig Schüler, Bryant He, H. Sch?ler, Lehti? L., Lari Lehtiö ORCID, Tobias Karlberg, Thomas Helleday ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The PARP-3 protein is closely related to the PARP-1 and PARP-2 proteins, which are involved in DNA repair and genome maintenance. Here, we characterized the biochemical properties of human PARP-3. PARP-3 is able to ADP-ribosylate itself as well as histone H1, a previously unknown substrate for PARP-3. PARP-3 is not activated upon binding to DNA and is a mono-ADP-ribosylase, in contrast to PARP-1 and PARP-2. PARP-3 interacts with PARP-1 and activates PARP-1 in the absence of DNA, resulting in synthesis of polymers of ADP-ribose. The N-terminal WGR domain of PARP-3 is involved in this activation. The functional interaction between PARP-3 and PARP-1 suggests that it may have a role in DNA repair. However, here we report that PARP-3 small interfering RNA-depleted cells are not sensitive to the topoisomerase I poison camptothecin, inducing DNA single-strand breaks, and repair these lesions as efficiently as wild-type cells. Altogether, these results suggest that the interaction between PARP-1 and PARP-3 is unrelated to DNA single-strand break repair.