Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro
Descripción del Articulo
Fondation ARC (http://www.arc-cancer.net) [PJA20151203415 to A.A.I.]; ERA.Net RUS Plus (www.eranet-rus.eu) [#306 to A.A.I. and RFBR-16-54-76010 to O.I.L.]; Electricité de France (http://www.edf.fr) [RB 2016-17 to M.K.S.]; Science Committee of the Ministry of Education and Science of the Republic of...
| Autores: | , , , , , , , , , , |
|---|---|
| Formato: | artículo |
| Fecha de Publicación: | 2016 |
| Institución: | Consejo Nacional de Ciencia Tecnología e Innovación |
| Repositorio: | CONCYTEC-Institucional |
| Lenguaje: | inglés |
| OAI Identifier: | oai:repositorio.concytec.gob.pe:20.500.12390/742 |
| Enlace del recurso: | https://hdl.handle.net/20.500.12390/742 https://doi.org/10.1093/nar/gkw675 |
| Nivel de acceso: | acceso abierto |
| Materia: | monomer cordycepin DNA fragment double stranded DNA glycosidase https://purl.org/pe-repo/ocde/ford#1.04.00 |
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| dc.title.none.fl_str_mv |
Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro |
| title |
Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro |
| spellingShingle |
Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro Talhaoui I. monomer cordycepin DNA fragment double stranded DNA glycosidase https://purl.org/pe-repo/ocde/ford#1.04.00 |
| title_short |
Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro |
| title_full |
Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro |
| title_fullStr |
Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro |
| title_full_unstemmed |
Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro |
| title_sort |
Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro |
| author |
Talhaoui I. |
| author_facet |
Talhaoui I. Lebedeva N.A. Zarkovic G. Saint-Pierre C. Kutuzov M.M. Sukhanova M.V. Matkarimov B.T. Gasparutto D. Saparbaev M.K. Lavrik O.I. Ishchenko A.A. |
| author_role |
author |
| author2 |
Lebedeva N.A. Zarkovic G. Saint-Pierre C. Kutuzov M.M. Sukhanova M.V. Matkarimov B.T. Gasparutto D. Saparbaev M.K. Lavrik O.I. Ishchenko A.A. |
| author2_role |
author author author author author author author author author author |
| dc.contributor.author.fl_str_mv |
Talhaoui I. Lebedeva N.A. Zarkovic G. Saint-Pierre C. Kutuzov M.M. Sukhanova M.V. Matkarimov B.T. Gasparutto D. Saparbaev M.K. Lavrik O.I. Ishchenko A.A. |
| dc.subject.none.fl_str_mv |
monomer |
| topic |
monomer cordycepin DNA fragment double stranded DNA glycosidase https://purl.org/pe-repo/ocde/ford#1.04.00 |
| dc.subject.es_PE.fl_str_mv |
cordycepin DNA fragment double stranded DNA glycosidase |
| dc.subject.ocde.none.fl_str_mv |
https://purl.org/pe-repo/ocde/ford#1.04.00 |
| description |
Fondation ARC (http://www.arc-cancer.net) [PJA20151203415 to A.A.I.]; ERA.Net RUS Plus (www.eranet-rus.eu) [#306 to A.A.I. and RFBR-16-54-76010 to O.I.L.]; Electricité de France (http://www.edf.fr) [RB 2016-17 to M.K.S.]; Science Committee of the Ministry of Education and Science of the Republic of Kazakhstan (program 0212/PTF-14-OT) [3755/GF4 and 2835/GF3] (http://www.nu.edu.kz) to B.T.M.; RSF [14-24-00038 to O.I.L.]; RFBR [15-54-16003]; Program of RAS on Molecular and Cellular Biology [6.4]; postdoctoral and doctoral fellowships from Fondation ARC (http://www.arc-cancer.net) [PDF20110603195 to I.T. and G.Z.] and CIENCIACTIVA/CONCYTEC (www.cienciactiva.gob.pe), respectively. Funding for open access charge: National Laboratory Astana, Nazarbayev University, Astana, Republic of Kazakhstan. |
| publishDate |
2016 |
| 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 |
2016 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article |
| format |
article |
| dc.identifier.uri.none.fl_str_mv |
https://hdl.handle.net/20.500.12390/742 |
| dc.identifier.doi.none.fl_str_mv |
https://doi.org/10.1093/nar/gkw675 |
| dc.identifier.scopus.none.fl_str_mv |
2-s2.0-84994817680 |
| url |
https://hdl.handle.net/20.500.12390/742 https://doi.org/10.1093/nar/gkw675 |
| identifier_str_mv |
2-s2.0-84994817680 |
| 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 |
| dc.rights.uri.none.fl_str_mv |
http://creativecommons.org/licenses/by-nc/4.0/ |
| eu_rights_str_mv |
openAccess |
| rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc/4.0/ |
| 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 |
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CONCYTEC |
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CONCYTEC |
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CONCYTEC-Institucional |
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CONCYTEC-Institucional |
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Repositorio Institucional CONCYTEC |
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repositorio@concytec.gob.pe |
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1839175759081504768 |
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Publicationrp00968500rp01893600rp00967500rp00962500rp00964500rp01894600rp00966500rp00965500rp01892600rp00961500rp00960500Talhaoui I.Lebedeva N.A.Zarkovic G.Saint-Pierre C.Kutuzov M.M.Sukhanova M.V.Matkarimov B.T.Gasparutto D.Saparbaev M.K.Lavrik O.I.Ishchenko A.A.2024-05-30T23:13:38Z2024-05-30T23:13:38Z2016https://hdl.handle.net/20.500.12390/742https://doi.org/10.1093/nar/gkw6752-s2.0-84994817680Fondation ARC (http://www.arc-cancer.net) [PJA20151203415 to A.A.I.]; ERA.Net RUS Plus (www.eranet-rus.eu) [#306 to A.A.I. and RFBR-16-54-76010 to O.I.L.]; Electricité de France (http://www.edf.fr) [RB 2016-17 to M.K.S.]; Science Committee of the Ministry of Education and Science of the Republic of Kazakhstan (program 0212/PTF-14-OT) [3755/GF4 and 2835/GF3] (http://www.nu.edu.kz) to B.T.M.; RSF [14-24-00038 to O.I.L.]; RFBR [15-54-16003]; Program of RAS on Molecular and Cellular Biology [6.4]; postdoctoral and doctoral fellowships from Fondation ARC (http://www.arc-cancer.net) [PDF20110603195 to I.T. and G.Z.] and CIENCIACTIVA/CONCYTEC (www.cienciactiva.gob.pe), respectively. Funding for open access charge: National Laboratory Astana, Nazarbayev University, Astana, Republic of Kazakhstan.Poly(ADP-ribose) polymerases (PARPs/ARTDs) use nicotinamide adenine dinucleotide (NAD+) to catalyse the synthesis of a long branched poly(ADP-ribose) polymer (PAR) attached to the acceptor amino acid residues of nuclear proteins. PARPs act on single- and double-stranded DNA breaks by recruiting DNA repair factors. Here, in in vitro biochemical experiments, we found that the mammalian PARP1 and PARP2 proteins can directly ADP-ribosylate the termini of DNA oligonucleotides. PARP1 preferentially catalysed covalent attachment of ADP-ribose units to the ends of recessed DNA duplexes containing 3′-cordycepin, 5′- and 3′-phosphate and also to 5′-phosphate of a single-stranded oligonucleotide. PARP2 preferentially ADP-ribosylated the nicked/gapped DNA duplexes containing 5′-phosphate at the double-stranded termini. PAR glycohydrolase (PARG) restored native DNA structure by hydrolysing PAR-DNA adducts generated by PARP1 and PARP2. Biochemical and mass spectrometry analyses of the adducts suggested that PARPs utilise DNA termini as an alternative to 2′-hydroxyl of ADP-ribose and protein acceptor residues to catalyse PAR chain initiation either via the 2′,1″-O-glycosidic ribose-ribose bond or via phosphodiester bond formation between C1′ of ADP-ribose and the phosphate of a terminal deoxyribonucleotide. This new type of post-replicative modification of DNA provides novel insights into the molecular mechanisms underlying biological phenomena of ADP-ribosylation mediated by PARPs.Consejo Nacional de Ciencia, Tecnología e Innovación Tecnológica - ConcytecengOxford University PressNucleic Acids Researchinfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc/4.0/monomercordycepin-1DNA fragment-1double stranded DNA-1glycosidase-1https://purl.org/pe-repo/ocde/ford#1.04.00-1Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitroinfo: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##PLACEHOLDER_PARENT_METADATA_VALUE#20.500.12390/742oai:repositorio.concytec.gob.pe:20.500.12390/7422024-05-30 15:22:47.647http://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccesshttp://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##PLACEHOLDER_PARENT_METADATA_VALUE#<Publication xmlns="https://www.openaire.eu/cerif-profile/1.1/" id="cf7ce5c2-2fef-498b-9105-8c4628cb1205"> <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>Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro</Title> <PublishedIn> <Publication> <Title>Nucleic Acids Research</Title> </Publication> </PublishedIn> <PublicationDate>2016</PublicationDate> <DOI>https://doi.org/10.1093/nar/gkw675</DOI> <SCP-Number>2-s2.0-84994817680</SCP-Number> <Authors> <Author> <DisplayName>Talhaoui I.</DisplayName> <Person id="rp00968" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Lebedeva N.A.</DisplayName> <Person id="rp01893" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Zarkovic G.</DisplayName> <Person id="rp00967" /> <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>Sukhanova M.V.</DisplayName> <Person id="rp01894" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Matkarimov B.T.</DisplayName> <Person id="rp00966" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Gasparutto D.</DisplayName> <Person id="rp00965" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Saparbaev M.K.</DisplayName> <Person id="rp01892" /> <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> <License>http://creativecommons.org/licenses/by-nc/4.0/</License> <Keyword>monomer</Keyword> <Keyword>cordycepin</Keyword> <Keyword>DNA fragment</Keyword> <Keyword>double stranded DNA</Keyword> <Keyword>glycosidase</Keyword> <Abstract>Poly(ADP-ribose) polymerases (PARPs/ARTDs) use nicotinamide adenine dinucleotide (NAD+) to catalyse the synthesis of a long branched poly(ADP-ribose) polymer (PAR) attached to the acceptor amino acid residues of nuclear proteins. PARPs act on single- and double-stranded DNA breaks by recruiting DNA repair factors. Here, in in vitro biochemical experiments, we found that the mammalian PARP1 and PARP2 proteins can directly ADP-ribosylate the termini of DNA oligonucleotides. PARP1 preferentially catalysed covalent attachment of ADP-ribose units to the ends of recessed DNA duplexes containing 3′-cordycepin, 5′- and 3′-phosphate and also to 5′-phosphate of a single-stranded oligonucleotide. PARP2 preferentially ADP-ribosylated the nicked/gapped DNA duplexes containing 5′-phosphate at the double-stranded termini. PAR glycohydrolase (PARG) restored native DNA structure by hydrolysing PAR-DNA adducts generated by PARP1 and PARP2. Biochemical and mass spectrometry analyses of the adducts suggested that PARPs utilise DNA termini as an alternative to 2′-hydroxyl of ADP-ribose and protein acceptor residues to catalyse PAR chain initiation either via the 2′,1″-O-glycosidic ribose-ribose bond or via phosphodiester bond formation between C1′ of ADP-ribose and the phosphate of a terminal deoxyribonucleotide. This new type of post-replicative modification of DNA provides novel insights into the molecular mechanisms underlying biological phenomena of ADP-ribosylation mediated by PARPs.</Abstract> <Access xmlns="http://purl.org/coar/access_right" > </Access> </Publication> -1 |
| score |
13.441383 |
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).
