Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent
- Autores
- Roberts, Irma; Tam Lam, Xuan; Miranda, Helder; Kieselbach, Thomas; Funk, Christiane
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The widely distributed members of the Deg/HtrA protease family play an important role in the proteolysis of misfolded and damaged proteins. Here we show that the Deg protease rHhoA is able to degrade PsbO, the extrinsic protein of the Photosystem II (PSII) oxygen-evolving complex in Synechocystis sp. PCC 6803 and in spinach. PsbO is known to be stable in its oxidized form, but after reduction by thioredoxin it became a substrate for recombinant HhoA (rHhoA). rHhoA cleaved reduced eukaryotic (specifically, spinach) PsbO at defined sites and created distinct PsbO fragments that were not further degraded. As for the corresponding prokaryotic substrate (reduced PsbO of Synechocystis sp. PCC 6803), no PsbO fragments were observed. Assembly to PSII protected PsbO from degradation. For Synechocystis sp. PCC 6803, our results show that HhoA, HhoB, and HtrA are localized in the periplasma and/or at the thylakoid membrane. In agreement with the idea that PsbO could be a physiological substrate for Deg proteases, part of the cellular fraction of the three Deg proteases of Synechocystis sp. PCC 6803 (HhoA, HhoB, and HtrA) was detected in the PSII-enriched membrane fraction.
Fil: Roberts, Irma. Universidad de Umea; Suecia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; Argentina
Fil: Tam Lam, Xuan. Universidad de Umea; Suecia
Fil: Miranda, Helder. Universidad de Umea; Suecia
Fil: Kieselbach, Thomas. Universidad de Umea; Suecia
Fil: Funk, Christiane. Universidad de Umea; Suecia - Materia
-
DEG PROTEASES
SYNECHOCYSTIS
PSBO
THIOREDOXIN - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/59665
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Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin DependentRoberts, IrmaTam Lam, XuanMiranda, HelderKieselbach, ThomasFunk, ChristianeDEG PROTEASESSYNECHOCYSTISPSBOTHIOREDOXINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The widely distributed members of the Deg/HtrA protease family play an important role in the proteolysis of misfolded and damaged proteins. Here we show that the Deg protease rHhoA is able to degrade PsbO, the extrinsic protein of the Photosystem II (PSII) oxygen-evolving complex in Synechocystis sp. PCC 6803 and in spinach. PsbO is known to be stable in its oxidized form, but after reduction by thioredoxin it became a substrate for recombinant HhoA (rHhoA). rHhoA cleaved reduced eukaryotic (specifically, spinach) PsbO at defined sites and created distinct PsbO fragments that were not further degraded. As for the corresponding prokaryotic substrate (reduced PsbO of Synechocystis sp. PCC 6803), no PsbO fragments were observed. Assembly to PSII protected PsbO from degradation. For Synechocystis sp. PCC 6803, our results show that HhoA, HhoB, and HtrA are localized in the periplasma and/or at the thylakoid membrane. In agreement with the idea that PsbO could be a physiological substrate for Deg proteases, part of the cellular fraction of the three Deg proteases of Synechocystis sp. PCC 6803 (HhoA, HhoB, and HtrA) was detected in the PSII-enriched membrane fraction.Fil: Roberts, Irma. Universidad de Umea; Suecia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; ArgentinaFil: Tam Lam, Xuan. Universidad de Umea; SueciaFil: Miranda, Helder. Universidad de Umea; SueciaFil: Kieselbach, Thomas. Universidad de Umea; SueciaFil: Funk, Christiane. Universidad de Umea; SueciaPublic Library of Science2012-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/59665Roberts, Irma; Tam Lam, Xuan; Miranda, Helder; Kieselbach, Thomas; Funk, Christiane; Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent; Public Library of Science; Plos One; 7; 9; 9-2012; 1-131932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0045713info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0045713info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:46:14Zoai:ri.conicet.gov.ar:11336/59665instacron: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 09:46:14.585CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent |
title |
Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent |
spellingShingle |
Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent Roberts, Irma DEG PROTEASES SYNECHOCYSTIS PSBO THIOREDOXIN |
title_short |
Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent |
title_full |
Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent |
title_fullStr |
Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent |
title_full_unstemmed |
Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent |
title_sort |
Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent |
dc.creator.none.fl_str_mv |
Roberts, Irma Tam Lam, Xuan Miranda, Helder Kieselbach, Thomas Funk, Christiane |
author |
Roberts, Irma |
author_facet |
Roberts, Irma Tam Lam, Xuan Miranda, Helder Kieselbach, Thomas Funk, Christiane |
author_role |
author |
author2 |
Tam Lam, Xuan Miranda, Helder Kieselbach, Thomas Funk, Christiane |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
DEG PROTEASES SYNECHOCYSTIS PSBO THIOREDOXIN |
topic |
DEG PROTEASES SYNECHOCYSTIS PSBO THIOREDOXIN |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The widely distributed members of the Deg/HtrA protease family play an important role in the proteolysis of misfolded and damaged proteins. Here we show that the Deg protease rHhoA is able to degrade PsbO, the extrinsic protein of the Photosystem II (PSII) oxygen-evolving complex in Synechocystis sp. PCC 6803 and in spinach. PsbO is known to be stable in its oxidized form, but after reduction by thioredoxin it became a substrate for recombinant HhoA (rHhoA). rHhoA cleaved reduced eukaryotic (specifically, spinach) PsbO at defined sites and created distinct PsbO fragments that were not further degraded. As for the corresponding prokaryotic substrate (reduced PsbO of Synechocystis sp. PCC 6803), no PsbO fragments were observed. Assembly to PSII protected PsbO from degradation. For Synechocystis sp. PCC 6803, our results show that HhoA, HhoB, and HtrA are localized in the periplasma and/or at the thylakoid membrane. In agreement with the idea that PsbO could be a physiological substrate for Deg proteases, part of the cellular fraction of the three Deg proteases of Synechocystis sp. PCC 6803 (HhoA, HhoB, and HtrA) was detected in the PSII-enriched membrane fraction. Fil: Roberts, Irma. Universidad de Umea; Suecia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; Argentina Fil: Tam Lam, Xuan. Universidad de Umea; Suecia Fil: Miranda, Helder. Universidad de Umea; Suecia Fil: Kieselbach, Thomas. Universidad de Umea; Suecia Fil: Funk, Christiane. Universidad de Umea; Suecia |
description |
The widely distributed members of the Deg/HtrA protease family play an important role in the proteolysis of misfolded and damaged proteins. Here we show that the Deg protease rHhoA is able to degrade PsbO, the extrinsic protein of the Photosystem II (PSII) oxygen-evolving complex in Synechocystis sp. PCC 6803 and in spinach. PsbO is known to be stable in its oxidized form, but after reduction by thioredoxin it became a substrate for recombinant HhoA (rHhoA). rHhoA cleaved reduced eukaryotic (specifically, spinach) PsbO at defined sites and created distinct PsbO fragments that were not further degraded. As for the corresponding prokaryotic substrate (reduced PsbO of Synechocystis sp. PCC 6803), no PsbO fragments were observed. Assembly to PSII protected PsbO from degradation. For Synechocystis sp. PCC 6803, our results show that HhoA, HhoB, and HtrA are localized in the periplasma and/or at the thylakoid membrane. In agreement with the idea that PsbO could be a physiological substrate for Deg proteases, part of the cellular fraction of the three Deg proteases of Synechocystis sp. PCC 6803 (HhoA, HhoB, and HtrA) was detected in the PSII-enriched membrane fraction. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-09 |
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/11336/59665 Roberts, Irma; Tam Lam, Xuan; Miranda, Helder; Kieselbach, Thomas; Funk, Christiane; Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent; Public Library of Science; Plos One; 7; 9; 9-2012; 1-13 1932-6203 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/59665 |
identifier_str_mv |
Roberts, Irma; Tam Lam, Xuan; Miranda, Helder; Kieselbach, Thomas; Funk, Christiane; Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent; Public Library of Science; Plos One; 7; 9; 9-2012; 1-13 1932-6203 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://journals.plos.org/plosone/article?id=10.1371/journal.pone.0045713 info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0045713 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Public Library of Science |
publisher.none.fl_str_mv |
Public Library of Science |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.070432 |