The ADP-ribose hydrolase NUDT5 is important for DNA repair

DNA damage leads to rapid synthesis of poly(ADP-ribose) (pADPr), which is important for damage signaling and repair. pADPr chains are removed by poly(ADP-ribose) glycohydrolase (PARG), releasing free mono(ADP-ribose) (mADPr). Here, we show that the NUDIX hydrolase NUDT5, which can hydrolyze mADPr to...

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Detalhes bibliográficos
Autores: Qi, Hongyun, Wright, Roni H.G., Beato, Miguel, Price, Brendan D.
Tipo de documento: artigo
Estado:Versão publicada
Data de publicação:2022
País:España
Recursos:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositório:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10230/55868
Acesso em linha:http://hdl.handle.net/10230/55868
http://dx.doi.org/10.1016/j.celrep.2022.111866
Access Level:Acceso aberto
Palavra-chave:ATP
CP: Cell biology
CP: Molecular biology
DNA repair
NUDIX hydrolase
NUDT5
PARPs
Chromatin
Energy metabolism
Homologous recombination
Mono(ADP-ribose)
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spelling The ADP-ribose hydrolase NUDT5 is important for DNA repairQi, HongyunWright, Roni H.G.Beato, MiguelPrice, Brendan D.ATPCP: Cell biologyCP: Molecular biologyDNA repairNUDIX hydrolaseNUDT5PARPsChromatinEnergy metabolismHomologous recombinationMono(ADP-ribose)DNA damage leads to rapid synthesis of poly(ADP-ribose) (pADPr), which is important for damage signaling and repair. pADPr chains are removed by poly(ADP-ribose) glycohydrolase (PARG), releasing free mono(ADP-ribose) (mADPr). Here, we show that the NUDIX hydrolase NUDT5, which can hydrolyze mADPr to ribose-5-phosphate and either AMP or ATP, is recruited to damage sites through interaction with PARG. NUDT5 does not regulate PARP or PARG activity. Instead, loss of NUDT5 reduces basal cellular ATP levels and exacerbates the decrease in cellular ATP that occurs during DNA repair. Further, loss of NUDT5 activity impairs RAD51 recruitment, attenuates the phosphorylation of key DNA-repair proteins, and reduces both H2A.Z exchange at damage sites and repair by homologous recombination. The ability of NUDT5 to hydrolyze mADPr, and/or regulate cellular ATP, may therefore be important for efficient DNA repair. Targeting NUDT5 to disrupt PAR/mADPr and energy metabolism may be an effective anti-cancer strategy.Elsevier202320232022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/10230/55868http://dx.doi.org/10.1016/j.celrep.2022.111866reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésCell Rep. 2022 Dec 20;41(12):111866© 2022 The Author(s). This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).http://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:recercat.cat:10230/558682026-05-29T05:05:01Z
dc.title.none.fl_str_mv The ADP-ribose hydrolase NUDT5 is important for DNA repair
title The ADP-ribose hydrolase NUDT5 is important for DNA repair
spellingShingle The ADP-ribose hydrolase NUDT5 is important for DNA repair
Qi, Hongyun
ATP
CP: Cell biology
CP: Molecular biology
DNA repair
NUDIX hydrolase
NUDT5
PARPs
Chromatin
Energy metabolism
Homologous recombination
Mono(ADP-ribose)
title_short The ADP-ribose hydrolase NUDT5 is important for DNA repair
title_full The ADP-ribose hydrolase NUDT5 is important for DNA repair
title_fullStr The ADP-ribose hydrolase NUDT5 is important for DNA repair
title_full_unstemmed The ADP-ribose hydrolase NUDT5 is important for DNA repair
title_sort The ADP-ribose hydrolase NUDT5 is important for DNA repair
dc.creator.none.fl_str_mv Qi, Hongyun
Wright, Roni H.G.
Beato, Miguel
Price, Brendan D.
author Qi, Hongyun
author_facet Qi, Hongyun
Wright, Roni H.G.
Beato, Miguel
Price, Brendan D.
author_role author
author2 Wright, Roni H.G.
Beato, Miguel
Price, Brendan D.
author2_role author
author
author
dc.subject.none.fl_str_mv ATP
CP: Cell biology
CP: Molecular biology
DNA repair
NUDIX hydrolase
NUDT5
PARPs
Chromatin
Energy metabolism
Homologous recombination
Mono(ADP-ribose)
topic ATP
CP: Cell biology
CP: Molecular biology
DNA repair
NUDIX hydrolase
NUDT5
PARPs
Chromatin
Energy metabolism
Homologous recombination
Mono(ADP-ribose)
description DNA damage leads to rapid synthesis of poly(ADP-ribose) (pADPr), which is important for damage signaling and repair. pADPr chains are removed by poly(ADP-ribose) glycohydrolase (PARG), releasing free mono(ADP-ribose) (mADPr). Here, we show that the NUDIX hydrolase NUDT5, which can hydrolyze mADPr to ribose-5-phosphate and either AMP or ATP, is recruited to damage sites through interaction with PARG. NUDT5 does not regulate PARP or PARG activity. Instead, loss of NUDT5 reduces basal cellular ATP levels and exacerbates the decrease in cellular ATP that occurs during DNA repair. Further, loss of NUDT5 activity impairs RAD51 recruitment, attenuates the phosphorylation of key DNA-repair proteins, and reduces both H2A.Z exchange at damage sites and repair by homologous recombination. The ability of NUDT5 to hydrolyze mADPr, and/or regulate cellular ATP, may therefore be important for efficient DNA repair. Targeting NUDT5 to disrupt PAR/mADPr and energy metabolism may be an effective anti-cancer strategy.
publishDate 2022
dc.date.none.fl_str_mv 2022
2023
2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10230/55868
http://dx.doi.org/10.1016/j.celrep.2022.111866
url http://hdl.handle.net/10230/55868
http://dx.doi.org/10.1016/j.celrep.2022.111866
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Cell Rep. 2022 Dec 20;41(12):111866
dc.rights.none.fl_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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