Change search
ReferencesLink to record
Permanent link

Direct link
PARP-3 Is a Mono-ADP-ribosylase That Activates PARP-1 in the Absence of DNA
Show others and affiliations
2010 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 285, no 11, 8054-8060 p.Article in journal (Refereed) Published
Abstract [en]

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 ADPribose. 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.

Place, publisher, year, edition, pages
2010. Vol. 285, no 11, 8054-8060 p.
National Category
Natural Sciences
URN: urn:nbn:se:su:diva-50504DOI: 10.1074/jbc.M109.077834ISI: 000275413800023OAI: diva2:383543
authorCount :7Available from: 2011-01-05 Created: 2010-12-28 Last updated: 2011-01-05Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Helleday, Thomas
By organisation
Department of Genetics, Microbiology and Toxicology
In the same journal
Journal of Biological Chemistry
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 25 hits
ReferencesLink to record
Permanent link

Direct link