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DNA is a New Target of Parp3. / Belousova, E. A.; Ishchenko, A. A.; Lavrik, O. I.

In: Scientific Reports, Vol. 8, No. 1, 4176, 08.03.2018, p. 4176.

Research output: Contribution to journal › Article › peer-review

Harvard

Belousova, EA, Ishchenko, AA & Lavrik, OI 2018, 'DNA is a New Target of Parp3', Scientific Reports, vol. 8, no. 1, 4176, pp. 4176. https://doi.org/10.1038/s41598-018-22673-3

APA

Belousova, E. A., Ishchenko, A. A., & Lavrik, O. I. (2018). DNA is a New Target of Parp3. Scientific Reports, 8(1), 4176. [4176]. https://doi.org/10.1038/s41598-018-22673-3

Vancouver

Belousova EA, Ishchenko AA, Lavrik OI. DNA is a New Target of Parp3. Scientific Reports. 2018 Mar 8;8(1):4176. 4176. doi: 10.1038/s41598-018-22673-3

Author

Belousova, E. A. ; Ishchenko, A. A. ; Lavrik, O. I. / DNA is a New Target of Parp3. In: Scientific Reports. 2018 ; Vol. 8, No. 1. pp. 4176.

BibTeX

@article{f17a8ab83db54c3dacb51197906db77e,
title = "DNA is a New Target of Parp3",
abstract = "Most members of the poly(ADP-ribose)polymerase family, PARP family, have a catalytic activity that involves the transfer of ADP-ribose from a beta-NAD+-molecule to protein acceptors. It was recently discovered by Talhaoui et al. that DNA-dependent PARP1 and PARP2 can also modify DNA. Here, we demonstrate that DNA-dependent PARP3 can modify DNA and form a specific primed structure for further use by the repair proteins. We demonstrated that gapped DNA that was ADP-ribosylated by PARP3 could be ligated to double-stranded DNA by DNA ligases. Moreover, this ADP-ribosylated DNA could serve as a primed DNA substrate for PAR chain elongation by the purified proteins PARP1 and PARP2 as well as by cell-free extracts. We suggest that this ADP-ribose modification can be involved in cellular pathways that are important for cell survival in the process of double-strand break formation.",
keywords = "3P21.3, CELLULAR-RESPONSE, CLONING, DAMAGE, EXPRESSION, GENES, POLY(ADP-RIBOSE) POLYMERASES, PROGRESSION, PROTEIN ADP-RIBOSYLATION, STRAND BREAKS",
author = "Belousova, {E. A.} and Ishchenko, {A. A.} and Lavrik, {O. I.}",
note = "Publisher Copyright: {\textcopyright} 2018 The Author(s).",
year = "2018",
month = mar,
day = "8",
doi = "10.1038/s41598-018-22673-3",
language = "English",
volume = "8",
pages = "4176",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",
number = "1",

}

RIS

TY - JOUR

T1 - DNA is a New Target of Parp3

AU - Belousova, E. A.

AU - Ishchenko, A. A.

AU - Lavrik, O. I.

N1 - Publisher Copyright: © 2018 The Author(s).

PY - 2018/3/8

Y1 - 2018/3/8

N2 - Most members of the poly(ADP-ribose)polymerase family, PARP family, have a catalytic activity that involves the transfer of ADP-ribose from a beta-NAD+-molecule to protein acceptors. It was recently discovered by Talhaoui et al. that DNA-dependent PARP1 and PARP2 can also modify DNA. Here, we demonstrate that DNA-dependent PARP3 can modify DNA and form a specific primed structure for further use by the repair proteins. We demonstrated that gapped DNA that was ADP-ribosylated by PARP3 could be ligated to double-stranded DNA by DNA ligases. Moreover, this ADP-ribosylated DNA could serve as a primed DNA substrate for PAR chain elongation by the purified proteins PARP1 and PARP2 as well as by cell-free extracts. We suggest that this ADP-ribose modification can be involved in cellular pathways that are important for cell survival in the process of double-strand break formation.

AB - Most members of the poly(ADP-ribose)polymerase family, PARP family, have a catalytic activity that involves the transfer of ADP-ribose from a beta-NAD+-molecule to protein acceptors. It was recently discovered by Talhaoui et al. that DNA-dependent PARP1 and PARP2 can also modify DNA. Here, we demonstrate that DNA-dependent PARP3 can modify DNA and form a specific primed structure for further use by the repair proteins. We demonstrated that gapped DNA that was ADP-ribosylated by PARP3 could be ligated to double-stranded DNA by DNA ligases. Moreover, this ADP-ribosylated DNA could serve as a primed DNA substrate for PAR chain elongation by the purified proteins PARP1 and PARP2 as well as by cell-free extracts. We suggest that this ADP-ribose modification can be involved in cellular pathways that are important for cell survival in the process of double-strand break formation.

KW - 3P21.3

KW - CELLULAR-RESPONSE

KW - CLONING

KW - DAMAGE

KW - EXPRESSION

KW - GENES

KW - POLY(ADP-RIBOSE) POLYMERASES

KW - PROGRESSION

KW - PROTEIN ADP-RIBOSYLATION

KW - STRAND BREAKS

UR - http://www.scopus.com/inward/record.url?scp=85043363725&partnerID=8YFLogxK

U2 - 10.1038/s41598-018-22673-3

DO - 10.1038/s41598-018-22673-3

M3 - Article

C2 - 29520010

AN - SCOPUS:85043363725

VL - 8

SP - 4176

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

M1 - 4176

ER -

ID: 10426024