Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus

Autores
Mangialavori, Irene Cecilia
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
RecA ATPases are a family of proteins that catalyzes the exchange of complementary DNA regions via homologous recombination. They are conserved from bacteria to humans and are crucial for DNA damage repair and genetic diversity. In this work, Knadler et al. examine how ATP hydrolysis and divalent cations impact the recombinase activity of Saccharolobus solfataricus RadA protein (ssoRadA). They find that the ssoRadA-mediated strand exchange depends on ATPase activity. The presence of Manganese reduces ATPase activity and enhances strand exchange, while calcium inhibits ATPase activity by preventing ATP binding to the protein, yet destabilizes the nucleoprotein ssoRadA filaments, allowing strand exchange regardless of the ATPase activity. Although RecA ATPases are highly conserved, this research offers intriguing new evidence that each member of the family requires individual evaluation.
Fil: Mangialavori, Irene Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Materia
RECA ATPASES
MG BINDING SITE
ATPASE ACTIVITY
RAD A-SACCHAROLOBUS SOLFATARICUS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/227940
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricusMangialavori, Irene CeciliaRECA ATPASESMG BINDING SITEATPASE ACTIVITYRAD A-SACCHAROLOBUS SOLFATARICUShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1RecA ATPases are a family of proteins that catalyzes the exchange of complementary DNA regions via homologous recombination. They are conserved from bacteria to humans and are crucial for DNA damage repair and genetic diversity. In this work, Knadler et al. examine how ATP hydrolysis and divalent cations impact the recombinase activity of Saccharolobus solfataricus RadA protein (ssoRadA). They find that the ssoRadA-mediated strand exchange depends on ATPase activity. The presence of Manganese reduces ATPase activity and enhances strand exchange, while calcium inhibits ATPase activity by preventing ATP binding to the protein, yet destabilizes the nucleoprotein ssoRadA filaments, allowing strand exchange regardless of the ATPase activity. Although RecA ATPases are highly conserved, this research offers intriguing new evidence that each member of the family requires individual evaluation.Fil: Mangialavori, Irene Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaJournal of the Serbian Chemical Society2023-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/227940Mangialavori, Irene Cecilia; Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus; Journal of the Serbian Chemical Society; Bioscience Reports; 43; 6; 6-2023; 1-60144-84631573-4935CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://portlandpress.com/bioscirep/article/43/6/BSR20230058/233153/Commentary-on-Divalent-metal-cofactorsinfo:eu-repo/semantics/altIdentifier/doi/10.1042/BSR20230058info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:33:20Zoai:ri.conicet.gov.ar:11336/227940instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:33:21.119CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus
title Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus
spellingShingle Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus
Mangialavori, Irene Cecilia
RECA ATPASES
MG BINDING SITE
ATPASE ACTIVITY
RAD A-SACCHAROLOBUS SOLFATARICUS
title_short Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus
title_full Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus
title_fullStr Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus
title_full_unstemmed Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus
title_sort Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus
dc.creator.none.fl_str_mv Mangialavori, Irene Cecilia
author Mangialavori, Irene Cecilia
author_facet Mangialavori, Irene Cecilia
author_role author
dc.subject.none.fl_str_mv RECA ATPASES
MG BINDING SITE
ATPASE ACTIVITY
RAD A-SACCHAROLOBUS SOLFATARICUS
topic RECA ATPASES
MG BINDING SITE
ATPASE ACTIVITY
RAD A-SACCHAROLOBUS SOLFATARICUS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv RecA ATPases are a family of proteins that catalyzes the exchange of complementary DNA regions via homologous recombination. They are conserved from bacteria to humans and are crucial for DNA damage repair and genetic diversity. In this work, Knadler et al. examine how ATP hydrolysis and divalent cations impact the recombinase activity of Saccharolobus solfataricus RadA protein (ssoRadA). They find that the ssoRadA-mediated strand exchange depends on ATPase activity. The presence of Manganese reduces ATPase activity and enhances strand exchange, while calcium inhibits ATPase activity by preventing ATP binding to the protein, yet destabilizes the nucleoprotein ssoRadA filaments, allowing strand exchange regardless of the ATPase activity. Although RecA ATPases are highly conserved, this research offers intriguing new evidence that each member of the family requires individual evaluation.
Fil: Mangialavori, Irene Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
description RecA ATPases are a family of proteins that catalyzes the exchange of complementary DNA regions via homologous recombination. They are conserved from bacteria to humans and are crucial for DNA damage repair and genetic diversity. In this work, Knadler et al. examine how ATP hydrolysis and divalent cations impact the recombinase activity of Saccharolobus solfataricus RadA protein (ssoRadA). They find that the ssoRadA-mediated strand exchange depends on ATPase activity. The presence of Manganese reduces ATPase activity and enhances strand exchange, while calcium inhibits ATPase activity by preventing ATP binding to the protein, yet destabilizes the nucleoprotein ssoRadA filaments, allowing strand exchange regardless of the ATPase activity. Although RecA ATPases are highly conserved, this research offers intriguing new evidence that each member of the family requires individual evaluation.
publishDate 2023
dc.date.none.fl_str_mv 2023-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/227940
Mangialavori, Irene Cecilia; Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus; Journal of the Serbian Chemical Society; Bioscience Reports; 43; 6; 6-2023; 1-6
0144-8463
1573-4935
CONICET Digital
CONICET
url http://hdl.handle.net/11336/227940
identifier_str_mv Mangialavori, Irene Cecilia; Commentary on: Divalent metal cofactors differentially modulate RadA-mediated strand invasion and exchange in Saccharolobus solfataricus; Journal of the Serbian Chemical Society; Bioscience Reports; 43; 6; 6-2023; 1-6
0144-8463
1573-4935
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://portlandpress.com/bioscirep/article/43/6/BSR20230058/233153/Commentary-on-Divalent-metal-cofactors
info:eu-repo/semantics/altIdentifier/doi/10.1042/BSR20230058
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Journal of the Serbian Chemical Society
publisher.none.fl_str_mv Journal of the Serbian Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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