Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation

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Fondation ARC (http://www.arc-cancer.net) [PJA20151203415 to A.A.I.]; ERA.Net RUS Plus (www.eranet-rus.eu) [DNA PARYLATION #306 to A.A.I., RFBR-16–54-76010 to O.I.L.]; Ministry of Education and Science of the Republic of Kazakhstan [programs 0115RK02473 and 0115RK03029 to B.T.M.]; NU ORAU (http://ww...

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Detalles Bibliográficos
Autores: Zarkovic G., Belousova E.A., Talhaoui I., Saint-Pierre C., Kutuzov M.M., Matkarimov B.T., Biard D., Gasparutto D., Lavrik O.I., Ishchenko A.A.
Formato: artículo
Fecha de Publicación:2018
Institución:Consejo Nacional de Ciencia Tecnología e Innovación
Repositorio:CONCYTEC-Institucional
Lenguaje:inglés
OAI Identifier:oai:repositorio.concytec.gob.pe:20.500.12390/549
Enlace del recurso:https://hdl.handle.net/20.500.12390/549
https://doi.org/10.1093/nar/gkx1318
Nivel de acceso:acceso abierto
Materia:unclassified drug
bleomycin
DNA
genomic DNA
glycosidase
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 2
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 3
poly(adenosine diphosphate ribose)
Article
cell free system
controlled study
DNA damage
DNA modification
DNA replication
double stranded DNA break
enzyme active site
enzyme activity
enzyme mechanism
enzyme specificity
HeLa cell line
human
human cell
molecular weight
mono adenosine diphosphate ribosylation
priority journal
single stranded DNA break
https://purl.org/pe-repo/ocde/ford#3.01.02
id CONC_963191523cd61b8e5a2cd87ad22d4dce
oai_identifier_str oai:repositorio.concytec.gob.pe:20.500.12390/549
network_acronym_str CONC
network_name_str CONCYTEC-Institucional
repository_id_str 4689
dc.title.none.fl_str_mv Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation
title Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation
spellingShingle Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation
Zarkovic G.
unclassified drug
bleomycin
DNA
genomic DNA
glycosidase
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 2
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 3
poly(adenosine diphosphate ribose)
Article
cell free system
controlled study
DNA damage
DNA modification
DNA replication
double stranded DNA break
double stranded DNA break
enzyme active site
enzyme activity
enzyme mechanism
enzyme specificity
HeLa cell line
human
human cell
molecular weight
mono adenosine diphosphate ribosylation
priority journal
single stranded DNA break
https://purl.org/pe-repo/ocde/ford#3.01.02
title_short Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation
title_full Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation
title_fullStr Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation
title_full_unstemmed Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation
title_sort Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation
author Zarkovic G.
author_facet Zarkovic G.
Belousova E.A.
Talhaoui I.
Saint-Pierre C.
Kutuzov M.M.
Matkarimov B.T.
Biard D.
Gasparutto D.
Lavrik O.I.
Ishchenko A.A.
author_role author
author2 Belousova E.A.
Talhaoui I.
Saint-Pierre C.
Kutuzov M.M.
Matkarimov B.T.
Biard D.
Gasparutto D.
Lavrik O.I.
Ishchenko A.A.
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Zarkovic G.
Belousova E.A.
Talhaoui I.
Saint-Pierre C.
Kutuzov M.M.
Matkarimov B.T.
Biard D.
Gasparutto D.
Lavrik O.I.
Ishchenko A.A.
dc.subject.none.fl_str_mv unclassified drug
topic unclassified drug
bleomycin
DNA
genomic DNA
glycosidase
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 2
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 3
poly(adenosine diphosphate ribose)
Article
cell free system
controlled study
DNA damage
DNA modification
DNA replication
double stranded DNA break
double stranded DNA break
enzyme active site
enzyme activity
enzyme mechanism
enzyme specificity
HeLa cell line
human
human cell
molecular weight
mono adenosine diphosphate ribosylation
priority journal
single stranded DNA break
https://purl.org/pe-repo/ocde/ford#3.01.02
dc.subject.es_PE.fl_str_mv bleomycin
DNA
genomic DNA
glycosidase
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 2
nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 3
poly(adenosine diphosphate ribose)
Article
cell free system
controlled study
DNA damage
DNA modification
DNA replication
double stranded DNA break
double stranded DNA break
enzyme active site
enzyme activity
enzyme mechanism
enzyme specificity
HeLa cell line
human
human cell
molecular weight
mono adenosine diphosphate ribosylation
priority journal
single stranded DNA break
dc.subject.ocde.none.fl_str_mv https://purl.org/pe-repo/ocde/ford#3.01.02
description Fondation ARC (http://www.arc-cancer.net) [PJA20151203415 to A.A.I.]; ERA.Net RUS Plus (www.eranet-rus.eu) [DNA PARYLATION #306 to A.A.I., RFBR-16–54-76010 to O.I.L.]; Ministry of Education and Science of the Republic of Kazakhstan [programs 0115RK02473 and 0115RK03029 to B.T.M.]; NU ORAU (http://www.nu.edu.kz) (to B.T.M.); RSF Grant [14–24-00038 to O.I.L.]; French National Research Agency ‘Labex program’ [ARCANE project ANR-11-LABX-0003–01 to C.S.-P., D.G.]; Fondation ARC Postdoctoral Fellowship (http://www.arc-cancer.net) [PDF20110603195 to I.T.]; CIENCIACTIVA/CONCYTEC Doctoral Fellowship (www.cienciactiva.gob.pe) (to G.Z.). Funding for open access charge: National Laboratory Astana, Nazarbayev University, Astana, Republic of Kazakhstan.
publishDate 2018
dc.date.accessioned.none.fl_str_mv 2024-05-30T23:13:38Z
dc.date.available.none.fl_str_mv 2024-05-30T23:13:38Z
dc.date.issued.fl_str_mv 2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/20.500.12390/549
dc.identifier.doi.none.fl_str_mv https://doi.org/10.1093/nar/gkx1318
dc.identifier.scopus.none.fl_str_mv 2-s2.0-85043399955
url https://hdl.handle.net/20.500.12390/549
https://doi.org/10.1093/nar/gkx1318
identifier_str_mv 2-s2.0-85043399955
dc.language.iso.none.fl_str_mv eng
language eng
dc.relation.ispartof.none.fl_str_mv Nucleic Acids Research
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:CONCYTEC-Institucional
instname:Consejo Nacional de Ciencia Tecnología e Innovación
instacron:CONCYTEC
instname_str Consejo Nacional de Ciencia Tecnología e Innovación
instacron_str CONCYTEC
institution CONCYTEC
reponame_str CONCYTEC-Institucional
collection CONCYTEC-Institucional
repository.name.fl_str_mv Repositorio Institucional CONCYTEC
repository.mail.fl_str_mv repositorio@concytec.gob.pe
_version_ 1844883035745419264
spelling Publicationrp00967600rp00959600rp00968600rp00962600rp00964600rp00966600rp00963600rp00965600rp00961600rp00960600Zarkovic G.Belousova E.A.Talhaoui I.Saint-Pierre C.Kutuzov M.M.Matkarimov B.T.Biard D.Gasparutto D.Lavrik O.I.Ishchenko A.A.2024-05-30T23:13:38Z2024-05-30T23:13:38Z2018https://hdl.handle.net/20.500.12390/549https://doi.org/10.1093/nar/gkx13182-s2.0-85043399955Fondation ARC (http://www.arc-cancer.net) [PJA20151203415 to A.A.I.]; ERA.Net RUS Plus (www.eranet-rus.eu) [DNA PARYLATION #306 to A.A.I., RFBR-16–54-76010 to O.I.L.]; Ministry of Education and Science of the Republic of Kazakhstan [programs 0115RK02473 and 0115RK03029 to B.T.M.]; NU ORAU (http://www.nu.edu.kz) (to B.T.M.); RSF Grant [14–24-00038 to O.I.L.]; French National Research Agency ‘Labex program’ [ARCANE project ANR-11-LABX-0003–01 to C.S.-P., D.G.]; Fondation ARC Postdoctoral Fellowship (http://www.arc-cancer.net) [PDF20110603195 to I.T.]; CIENCIACTIVA/CONCYTEC Doctoral Fellowship (www.cienciactiva.gob.pe) (to G.Z.). Funding for open access charge: National Laboratory Astana, Nazarbayev University, Astana, Republic of Kazakhstan.Poly(ADP-ribose) polymerases (PARPs) act as DNA break sensors and catalyze the synthesis of polymers of ADP-ribose (PAR) covalently attached to acceptor proteins at DNA damage sites. It has been demonstrated that both mammalian PARP1 and PARP2 PARylate double-strand break termini in DNA oligonucleotide duplexes in vitro. Here, we show that mammalian PARP2 and PARP3 can PARylate and mono(ADP-ribosyl)ate (MARylate), respectively, 5'- and 3'-terminal phosphate residues at double- and single-strand break termini of a DNA molecule containing multiple strand breaks. PARP3-catalyzed DNA MARylation can be considered a new type of reversible post-replicative DNA modification. According to DNA substrate specificity of PARP3 and PARP2, we propose a putative mechanistic model of PARP-catalyzed strand break-oriented ADP-ribosylation of DNA termini. Notably, PARP-mediated DNA ADP-ribosylation can be more effective than PARPs' auto-ADP-ribosylation depending on the DNA substrates and reaction conditions used. Finally, we show an effective PARP3- or PARP2-catalyzed ADP-ribosylation of high-molecular-weight (∼3-kb) DNA molecules, PARP-mediated DNA PARylation in cell-free extracts and a persisting signal of anti-PAR antibodies in a serially purified genomic DNA from bleomycin-treated poly(ADP-ribose) glycohydrolase-depleted HeLa cells. These results suggest that certain types of complex DNA breaks can be effectively ADP-ribosylated by PARPs in cellular response to DNA damage.Consejo Nacional de Ciencia, Tecnología e Innovación Tecnológica - ConcytecengOxford University PressNucleic Acids Researchinfo:eu-repo/semantics/openAccessunclassified drugbleomycin-1DNA-1genomic DNA-1glycosidase-1nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase-1nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 2-1nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 3-1poly(adenosine diphosphate ribose)-1Article-1cell free system-1controlled study-1DNA damage-1DNA modification-1DNA replication-1double stranded DNA break-1double stranded DNA break-1enzyme active site-1enzyme activity-1enzyme mechanism-1enzyme specificity-1HeLa cell line-1human-1human cell-1molecular weight-1mono adenosine diphosphate ribosylation-1priority journal-1single stranded DNA break-1https://purl.org/pe-repo/ocde/ford#3.01.02-1Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylationinfo:eu-repo/semantics/articlereponame:CONCYTEC-Institucionalinstname:Consejo Nacional de Ciencia Tecnología e Innovacióninstacron:CONCYTEC#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#20.500.12390/549oai:repositorio.concytec.gob.pe:20.500.12390/5492024-05-30 15:22:09.208http://purl.org/coar/access_right/c_14cbinfo:eu-repo/semantics/closedAccessmetadata only accesshttps://repositorio.concytec.gob.peRepositorio Institucional CONCYTECrepositorio@concytec.gob.pe#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#<Publication xmlns="https://www.openaire.eu/cerif-profile/1.1/" id="d6cd6b1d-156e-4c11-804d-267fafba53f1"> <Type xmlns="https://www.openaire.eu/cerif-profile/vocab/COAR_Publication_Types">http://purl.org/coar/resource_type/c_1843</Type> <Language>eng</Language> <Title>Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation</Title> <PublishedIn> <Publication> <Title>Nucleic Acids Research</Title> </Publication> </PublishedIn> <PublicationDate>2018</PublicationDate> <DOI>https://doi.org/10.1093/nar/gkx1318</DOI> <SCP-Number>2-s2.0-85043399955</SCP-Number> <Authors> <Author> <DisplayName>Zarkovic G.</DisplayName> <Person id="rp00967" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Belousova E.A.</DisplayName> <Person id="rp00959" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Talhaoui I.</DisplayName> <Person id="rp00968" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Saint-Pierre C.</DisplayName> <Person id="rp00962" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Kutuzov M.M.</DisplayName> <Person id="rp00964" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Matkarimov B.T.</DisplayName> <Person id="rp00966" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Biard D.</DisplayName> <Person id="rp00963" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Gasparutto D.</DisplayName> <Person id="rp00965" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Lavrik O.I.</DisplayName> <Person id="rp00961" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Ishchenko A.A.</DisplayName> <Person id="rp00960" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> </Authors> <Editors> </Editors> <Publishers> <Publisher> <DisplayName>Oxford University Press</DisplayName> <OrgUnit /> </Publisher> </Publishers> <Keyword>unclassified drug</Keyword> <Keyword>bleomycin</Keyword> <Keyword>DNA</Keyword> <Keyword>genomic DNA</Keyword> <Keyword>glycosidase</Keyword> <Keyword>nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase</Keyword> <Keyword>nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 2</Keyword> <Keyword>nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase 3</Keyword> <Keyword>poly(adenosine diphosphate ribose)</Keyword> <Keyword>Article</Keyword> <Keyword>cell free system</Keyword> <Keyword>controlled study</Keyword> <Keyword>DNA damage</Keyword> <Keyword>DNA modification</Keyword> <Keyword>DNA replication</Keyword> <Keyword>double stranded DNA break</Keyword> <Keyword>double stranded DNA break</Keyword> <Keyword>enzyme active site</Keyword> <Keyword>enzyme activity</Keyword> <Keyword>enzyme mechanism</Keyword> <Keyword>enzyme specificity</Keyword> <Keyword>HeLa cell line</Keyword> <Keyword>human</Keyword> <Keyword>human cell</Keyword> <Keyword>molecular weight</Keyword> <Keyword>mono adenosine diphosphate ribosylation</Keyword> <Keyword>priority journal</Keyword> <Keyword>single stranded DNA break</Keyword> <Abstract>Poly(ADP-ribose) polymerases (PARPs) act as DNA break sensors and catalyze the synthesis of polymers of ADP-ribose (PAR) covalently attached to acceptor proteins at DNA damage sites. It has been demonstrated that both mammalian PARP1 and PARP2 PARylate double-strand break termini in DNA oligonucleotide duplexes in vitro. Here, we show that mammalian PARP2 and PARP3 can PARylate and mono(ADP-ribosyl)ate (MARylate), respectively, 5&apos;- and 3&apos;-terminal phosphate residues at double- and single-strand break termini of a DNA molecule containing multiple strand breaks. PARP3-catalyzed DNA MARylation can be considered a new type of reversible post-replicative DNA modification. According to DNA substrate specificity of PARP3 and PARP2, we propose a putative mechanistic model of PARP-catalyzed strand break-oriented ADP-ribosylation of DNA termini. Notably, PARP-mediated DNA ADP-ribosylation can be more effective than PARPs&apos; auto-ADP-ribosylation depending on the DNA substrates and reaction conditions used. Finally, we show an effective PARP3- or PARP2-catalyzed ADP-ribosylation of high-molecular-weight (∼3-kb) DNA molecules, PARP-mediated DNA PARylation in cell-free extracts and a persisting signal of anti-PAR antibodies in a serially purified genomic DNA from bleomycin-treated poly(ADP-ribose) glycohydrolase-depleted HeLa cells. These results suggest that certain types of complex DNA breaks can be effectively ADP-ribosylated by PARPs in cellular response to DNA damage.</Abstract> <Access xmlns="http://purl.org/coar/access_right" > </Access> </Publication> -1
score 13.425424
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