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PARP-3 Is a Mono-AD...
PARP-3 Is a Mono-ADP-ribosylase That Activates PARP-1 in the Absence of DNA
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Loseva, Olga (författare)
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Jemth, Ann-Sofie (författare)
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Bryant, Helen E. (författare)
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- Schuler, Herwig (författare)
- Karolinska Institutet
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Lehtio, Lari (författare)
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- Karlberg, Tobias (författare)
- Karolinska Institutet
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- Helleday, Thomas (författare)
- Stockholms universitet,Institutionen för genetik, mikrobiologi och toxikologi
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(creator_code:org_t)
- 2010
- 2010
- Engelska.
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 285:11, s. 8054-8060
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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http://kipublication...
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Abstract
Ämnesord
Stäng
- 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.
Nyckelord
- NATURAL SCIENCES
- NATURVETENSKAP
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