Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: New insights into DNA ADP-ribosylation
Descripción del Articulo
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...
| Autores: | , , , , , , , , , |
|---|---|
| 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 |
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| 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 |
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Consejo Nacional de Ciencia Tecnología e Innovación |
| instacron_str |
CONCYTEC |
| institution |
CONCYTEC |
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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'- 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.</Abstract> <Access xmlns="http://purl.org/coar/access_right" > </Access> </Publication> -1 |
| score |
13.425424 |
Nota importante:
La información contenida en este registro es de entera responsabilidad de la institución que gestiona el repositorio institucional donde esta contenido este documento o set de datos. El CONCYTEC no se hace responsable por los contenidos (publicaciones y/o datos) accesibles a través del Repositorio Nacional Digital de Ciencia, Tecnología e Innovación de Acceso Abierto (ALICIA).
La información contenida en este registro es de entera responsabilidad de la institución que gestiona el repositorio institucional donde esta contenido este documento o set de datos. El CONCYTEC no se hace responsable por los contenidos (publicaciones y/o datos) accesibles a través del Repositorio Nacional Digital de Ciencia, Tecnología e Innovación de Acceso Abierto (ALICIA).