Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity
- Autores
- Rajapaksha, Nimesha; Soldano, Anabel; Yao, Huili; Donnarumma, Fabrizio; Kashipathy, Maithri M.; Seibold, Steve; Battaile, Kevin P.; Lovell, Scott; Rivera, Mario
- Año de publicación
- 2023
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- We report the structural, biochemical, and functional characterization of the product of gene PA0962 from Pseudomonas aeruginosa PAO1. The protein, termed Pa Dps, adopts the Dps subunit fold and oligomerizes into a nearly spherical 12-mer quaternary structure at pH 6.0 or in the presence of divalent cations at neutral pH and above. The 12-Mer Pa Dps contains two di-iron centers at the interface of each subunit dimer, coordinated by conserved His, Glu, and Asp residues. In vitro, the di-iron centers catalyze the oxidation of Fe2+ utilizing H2O2 (not O2) as an oxidant, suggesting Pa Dps functions to aid P. aeruginosa to survive H2O2-mediated oxidative stress. In agreement, a P. aeruginosa Δdps mutant is significantly more susceptible to H2O2 than the parent strain. The Pa Dps structure harbors a novel network of Tyr residues at the interface of each subunit dimer between the two di-iron centers, which captures radicals generated during Fe2+ oxidation at the ferroxidase centers and forms di-tyrosine linkages, thus effectively trapping the radicals within the Dps shell. Surprisingly, incubating Pa Dps and DNA revealed unprecedented DNA cleaving activity that is independent of H2O2 or O2 but requires divalent cations and 12-mer Pa Dps.
Fil: Rajapaksha, Nimesha. State University of Louisiana; Estados Unidos
Fil: Soldano, Anabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina. State University of Louisiana; Estados Unidos
Fil: Yao, Huili. State University of Louisiana; Estados Unidos
Fil: Donnarumma, Fabrizio. State University of Louisiana; Estados Unidos
Fil: Kashipathy, Maithri M.. University of Kansas; Estados Unidos
Fil: Seibold, Steve. University of Kansas; Estados Unidos
Fil: Battaile, Kevin P.. New York Structural Biology Center; Estados Unidos
Fil: Lovell, Scott. University of Kansas; Estados Unidos
Fil: Rivera, Mario. State University of Louisiana; Estados Unidos - Materia
-
DNA CLEAVING ACTIVITY
DPS
EXONUCLEASE
FERRITIN
IRON METABOLISM
MINI FERRITIN
OXIDATIVE STRESS
PEROXIDE TOXICITY - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/226732
Ver los metadatos del registro completo
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Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving ActivityRajapaksha, NimeshaSoldano, AnabelYao, HuiliDonnarumma, FabrizioKashipathy, Maithri M.Seibold, SteveBattaile, Kevin P.Lovell, ScottRivera, MarioDNA CLEAVING ACTIVITYDPSEXONUCLEASEFERRITINIRON METABOLISMMINI FERRITINOXIDATIVE STRESSPEROXIDE TOXICITYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We report the structural, biochemical, and functional characterization of the product of gene PA0962 from Pseudomonas aeruginosa PAO1. The protein, termed Pa Dps, adopts the Dps subunit fold and oligomerizes into a nearly spherical 12-mer quaternary structure at pH 6.0 or in the presence of divalent cations at neutral pH and above. The 12-Mer Pa Dps contains two di-iron centers at the interface of each subunit dimer, coordinated by conserved His, Glu, and Asp residues. In vitro, the di-iron centers catalyze the oxidation of Fe2+ utilizing H2O2 (not O2) as an oxidant, suggesting Pa Dps functions to aid P. aeruginosa to survive H2O2-mediated oxidative stress. In agreement, a P. aeruginosa Δdps mutant is significantly more susceptible to H2O2 than the parent strain. The Pa Dps structure harbors a novel network of Tyr residues at the interface of each subunit dimer between the two di-iron centers, which captures radicals generated during Fe2+ oxidation at the ferroxidase centers and forms di-tyrosine linkages, thus effectively trapping the radicals within the Dps shell. Surprisingly, incubating Pa Dps and DNA revealed unprecedented DNA cleaving activity that is independent of H2O2 or O2 but requires divalent cations and 12-mer Pa Dps.Fil: Rajapaksha, Nimesha. State University of Louisiana; Estados UnidosFil: Soldano, Anabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina. State University of Louisiana; Estados UnidosFil: Yao, Huili. State University of Louisiana; Estados UnidosFil: Donnarumma, Fabrizio. State University of Louisiana; Estados UnidosFil: Kashipathy, Maithri M.. University of Kansas; Estados UnidosFil: Seibold, Steve. University of Kansas; Estados UnidosFil: Battaile, Kevin P.. New York Structural Biology Center; Estados UnidosFil: Lovell, Scott. University of Kansas; Estados UnidosFil: Rivera, Mario. State University of Louisiana; Estados UnidosMultidisciplinary Digital Publishing Institute2023-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/226732Rajapaksha, Nimesha; Soldano, Anabel; Yao, Huili; Donnarumma, Fabrizio; Kashipathy, Maithri M.; et al.; Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity; Multidisciplinary Digital Publishing Institute; International Journal of Molecular Sciences; 24; 5; 3-2023; 1-201661-65961422-0067CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1422-0067/24/5/4669info:eu-repo/semantics/altIdentifier/doi/10.3390/ijms24054669info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:08:38Zoai:ri.conicet.gov.ar:11336/226732instacron: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:34982025-10-22 12:08:38.54CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity |
| title |
Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity |
| spellingShingle |
Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity Rajapaksha, Nimesha DNA CLEAVING ACTIVITY DPS EXONUCLEASE FERRITIN IRON METABOLISM MINI FERRITIN OXIDATIVE STRESS PEROXIDE TOXICITY |
| title_short |
Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity |
| title_full |
Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity |
| title_fullStr |
Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity |
| title_full_unstemmed |
Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity |
| title_sort |
Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity |
| dc.creator.none.fl_str_mv |
Rajapaksha, Nimesha Soldano, Anabel Yao, Huili Donnarumma, Fabrizio Kashipathy, Maithri M. Seibold, Steve Battaile, Kevin P. Lovell, Scott Rivera, Mario |
| author |
Rajapaksha, Nimesha |
| author_facet |
Rajapaksha, Nimesha Soldano, Anabel Yao, Huili Donnarumma, Fabrizio Kashipathy, Maithri M. Seibold, Steve Battaile, Kevin P. Lovell, Scott Rivera, Mario |
| author_role |
author |
| author2 |
Soldano, Anabel Yao, Huili Donnarumma, Fabrizio Kashipathy, Maithri M. Seibold, Steve Battaile, Kevin P. Lovell, Scott Rivera, Mario |
| author2_role |
author author author author author author author author |
| dc.subject.none.fl_str_mv |
DNA CLEAVING ACTIVITY DPS EXONUCLEASE FERRITIN IRON METABOLISM MINI FERRITIN OXIDATIVE STRESS PEROXIDE TOXICITY |
| topic |
DNA CLEAVING ACTIVITY DPS EXONUCLEASE FERRITIN IRON METABOLISM MINI FERRITIN OXIDATIVE STRESS PEROXIDE TOXICITY |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| dc.description.none.fl_txt_mv |
We report the structural, biochemical, and functional characterization of the product of gene PA0962 from Pseudomonas aeruginosa PAO1. The protein, termed Pa Dps, adopts the Dps subunit fold and oligomerizes into a nearly spherical 12-mer quaternary structure at pH 6.0 or in the presence of divalent cations at neutral pH and above. The 12-Mer Pa Dps contains two di-iron centers at the interface of each subunit dimer, coordinated by conserved His, Glu, and Asp residues. In vitro, the di-iron centers catalyze the oxidation of Fe2+ utilizing H2O2 (not O2) as an oxidant, suggesting Pa Dps functions to aid P. aeruginosa to survive H2O2-mediated oxidative stress. In agreement, a P. aeruginosa Δdps mutant is significantly more susceptible to H2O2 than the parent strain. The Pa Dps structure harbors a novel network of Tyr residues at the interface of each subunit dimer between the two di-iron centers, which captures radicals generated during Fe2+ oxidation at the ferroxidase centers and forms di-tyrosine linkages, thus effectively trapping the radicals within the Dps shell. Surprisingly, incubating Pa Dps and DNA revealed unprecedented DNA cleaving activity that is independent of H2O2 or O2 but requires divalent cations and 12-mer Pa Dps. Fil: Rajapaksha, Nimesha. State University of Louisiana; Estados Unidos Fil: Soldano, Anabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina. State University of Louisiana; Estados Unidos Fil: Yao, Huili. State University of Louisiana; Estados Unidos Fil: Donnarumma, Fabrizio. State University of Louisiana; Estados Unidos Fil: Kashipathy, Maithri M.. University of Kansas; Estados Unidos Fil: Seibold, Steve. University of Kansas; Estados Unidos Fil: Battaile, Kevin P.. New York Structural Biology Center; Estados Unidos Fil: Lovell, Scott. University of Kansas; Estados Unidos Fil: Rivera, Mario. State University of Louisiana; Estados Unidos |
| description |
We report the structural, biochemical, and functional characterization of the product of gene PA0962 from Pseudomonas aeruginosa PAO1. The protein, termed Pa Dps, adopts the Dps subunit fold and oligomerizes into a nearly spherical 12-mer quaternary structure at pH 6.0 or in the presence of divalent cations at neutral pH and above. The 12-Mer Pa Dps contains two di-iron centers at the interface of each subunit dimer, coordinated by conserved His, Glu, and Asp residues. In vitro, the di-iron centers catalyze the oxidation of Fe2+ utilizing H2O2 (not O2) as an oxidant, suggesting Pa Dps functions to aid P. aeruginosa to survive H2O2-mediated oxidative stress. In agreement, a P. aeruginosa Δdps mutant is significantly more susceptible to H2O2 than the parent strain. The Pa Dps structure harbors a novel network of Tyr residues at the interface of each subunit dimer between the two di-iron centers, which captures radicals generated during Fe2+ oxidation at the ferroxidase centers and forms di-tyrosine linkages, thus effectively trapping the radicals within the Dps shell. Surprisingly, incubating Pa Dps and DNA revealed unprecedented DNA cleaving activity that is independent of H2O2 or O2 but requires divalent cations and 12-mer Pa Dps. |
| publishDate |
2023 |
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2023-03 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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http://hdl.handle.net/11336/226732 Rajapaksha, Nimesha; Soldano, Anabel; Yao, Huili; Donnarumma, Fabrizio; Kashipathy, Maithri M.; et al.; Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity; Multidisciplinary Digital Publishing Institute; International Journal of Molecular Sciences; 24; 5; 3-2023; 1-20 1661-6596 1422-0067 CONICET Digital CONICET |
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http://hdl.handle.net/11336/226732 |
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Rajapaksha, Nimesha; Soldano, Anabel; Yao, Huili; Donnarumma, Fabrizio; Kashipathy, Maithri M.; et al.; Pseudomonas aeruginosa Dps (PA0962) Functions in H2O2 Mediated Oxidative Stress Defense and Exhibits In Vitro DNA Cleaving Activity; Multidisciplinary Digital Publishing Institute; International Journal of Molecular Sciences; 24; 5; 3-2023; 1-20 1661-6596 1422-0067 CONICET Digital CONICET |
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eng |
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