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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/59665
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-10-22T11:15:03Zoai: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:34982025-10-22 11:15:03.654CONICET 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
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 12.982451

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