Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent

Autores
Roberts, Irma N.; Lam, Xuan Tam; Miranda, Helder; Kieselbach, Thomas; Funk, Christiane
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Roberts, Irma N. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales (INBA). Buenos Aires, Argentina.
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.
Fuente
Plos One
Vol.7, no.9
e45713
http://www.plos.org/
Materia
BACTERIAL PROTEIN
DEG PROTEASE RECOMBINANT HHOA
PROTEIN HHOA
PROTEIN HHOB
PROTEIN HTRA
PROTEIN PSBO
THIOREDOXIN
UNCLASSIFIED DRUG
BACTERIAL CELL
BACTERIAL STRAIN
CELL FRACTIONATION
CELLULAR DISTRIBUTION
CONTROLLED STUDY
CYTOPLASM
ENZYME DEGRADATION
ENZYME SUBSTRATE
EUKARYOTE
NONHUMAN
NUCLEOTIDE SEQUENCE
OXIDATION REDUCTION REACTION
PHOTOSYSTEM II
PROKARYOTE
PROTEIN ASSEMBLY
PROTEIN CLEAVAGE
PROTEIN LOCALIZATION
SPINACH
SYNECHOCOCCUS
THYLAKOID MEMBRANE
AMINO ACID SEQUENCE
BACTERIAL PROTEINS
BASE SEQUENCE
BLOTTING, WESTERN
DNA PRIMERS
ELECTROPHORESIS, POLYACRYLAMIDE GEL
KINETICS
MASS SPECTROMETRY
MOLECULAR SEQUENCE DATA
PROTEOLYSIS
RECOMBINANT PROTEINS
SUBCELLULAR FRACTIONS
SUBSTRATE SPECIFICITY
SYNECHOCYSTIS
THIOREDOXINS
EUKARYOTA
PROKARYOTA
SPINACIA OLERACEA
SYNECHOCYSTIS SP. PCC 6803
Nivel de accesibilidad
acceso abierto
Condiciones de uso
acceso abierto
Repositorio
FAUBA Digital (UBA-FAUBA)
Institución
Universidad de Buenos Aires. Facultad de Agronomía
OAI Identificador
snrd:2012Roberts

id FAUBA_3c4a86564f5e41d82c28670589582f6b
oai_identifier_str snrd:2012Roberts
network_acronym_str FAUBA
repository_id_str 2729
network_name_str FAUBA Digital (UBA-FAUBA)
spelling Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin DependentRoberts, Irma N.Lam, Xuan TamMiranda, HelderKieselbach, ThomasFunk, ChristianeBACTERIAL PROTEINDEG PROTEASE RECOMBINANT HHOAPROTEIN HHOAPROTEIN HHOBPROTEIN HTRAPROTEIN PSBOTHIOREDOXINUNCLASSIFIED DRUGBACTERIAL CELLBACTERIAL STRAINCELL FRACTIONATIONCELLULAR DISTRIBUTIONCONTROLLED STUDYCYTOPLASMENZYME DEGRADATIONENZYME SUBSTRATEEUKARYOTENONHUMANNUCLEOTIDE SEQUENCEOXIDATION REDUCTION REACTIONPHOTOSYSTEM IIPROKARYOTEPROTEIN ASSEMBLYPROTEIN CLEAVAGEPROTEIN LOCALIZATIONSPINACHSYNECHOCOCCUSTHYLAKOID MEMBRANEAMINO ACID SEQUENCEBACTERIAL PROTEINSBASE SEQUENCEBLOTTING, WESTERNDNA PRIMERSELECTROPHORESIS, POLYACRYLAMIDE GELKINETICSMASS SPECTROMETRYMOLECULAR SEQUENCE DATAPROTEOLYSISRECOMBINANT PROTEINSSUBCELLULAR FRACTIONSSUBSTRATE SPECIFICITYSYNECHOCYSTISTHIOREDOXINSEUKARYOTAPROKARYOTASPINACIA OLERACEASYNECHOCYSTIS SP. PCC 6803Fil: Roberts, Irma N. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales (INBA). Buenos Aires, Argentina.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.2012articleinfo:eu-repo/semantics/articlepublishedVersioninfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfdoi:10.1371/journal.pone.0045713issn:1932-6203http://ri.agro.uba.ar/greenstone3/library/collection/arti/document/2012RobertsPlos OneVol.7, no.9e45713http://www.plos.org/reponame:FAUBA Digital (UBA-FAUBA)instname:Universidad de Buenos Aires. Facultad de Agronomíaenginfo:eu-repo/semantics/openAccessopenAccesshttp://ri.agro.uba.ar/greenstone3/library/page/biblioteca#section42025-09-29T13:41:16Zsnrd:2012Robertsinstacron:UBA-FAUBAInstitucionalhttp://ri.agro.uba.ar/Universidad públicaNo correspondehttp://ri.agro.uba.ar/greenstone3/oaiserver?verb=ListSetsmartino@agro.uba.ar;berasa@agro.uba.ar ArgentinaNo correspondeNo correspondeNo correspondeopendoar:27292025-09-29 13:41:17.388FAUBA Digital (UBA-FAUBA) - Universidad de Buenos Aires. Facultad de Agronomíafalse
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 N.
BACTERIAL PROTEIN
DEG PROTEASE RECOMBINANT HHOA
PROTEIN HHOA
PROTEIN HHOB
PROTEIN HTRA
PROTEIN PSBO
THIOREDOXIN
UNCLASSIFIED DRUG
BACTERIAL CELL
BACTERIAL STRAIN
CELL FRACTIONATION
CELLULAR DISTRIBUTION
CONTROLLED STUDY
CYTOPLASM
ENZYME DEGRADATION
ENZYME SUBSTRATE
EUKARYOTE
NONHUMAN
NUCLEOTIDE SEQUENCE
OXIDATION REDUCTION REACTION
PHOTOSYSTEM II
PROKARYOTE
PROTEIN ASSEMBLY
PROTEIN CLEAVAGE
PROTEIN LOCALIZATION
SPINACH
SYNECHOCOCCUS
THYLAKOID MEMBRANE
AMINO ACID SEQUENCE
BACTERIAL PROTEINS
BASE SEQUENCE
BLOTTING, WESTERN
DNA PRIMERS
ELECTROPHORESIS, POLYACRYLAMIDE GEL
KINETICS
MASS SPECTROMETRY
MOLECULAR SEQUENCE DATA
PROTEOLYSIS
RECOMBINANT PROTEINS
SUBCELLULAR FRACTIONS
SUBSTRATE SPECIFICITY
SYNECHOCYSTIS
THIOREDOXINS
EUKARYOTA
PROKARYOTA
SPINACIA OLERACEA
SYNECHOCYSTIS SP. PCC 6803
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 N.
Lam, Xuan Tam
Miranda, Helder
Kieselbach, Thomas
Funk, Christiane
author Roberts, Irma N.
author_facet Roberts, Irma N.
Lam, Xuan Tam
Miranda, Helder
Kieselbach, Thomas
Funk, Christiane
author_role author
author2 Lam, Xuan Tam
Miranda, Helder
Kieselbach, Thomas
Funk, Christiane
author2_role author
author
author
author
dc.subject.none.fl_str_mv BACTERIAL PROTEIN
DEG PROTEASE RECOMBINANT HHOA
PROTEIN HHOA
PROTEIN HHOB
PROTEIN HTRA
PROTEIN PSBO
THIOREDOXIN
UNCLASSIFIED DRUG
BACTERIAL CELL
BACTERIAL STRAIN
CELL FRACTIONATION
CELLULAR DISTRIBUTION
CONTROLLED STUDY
CYTOPLASM
ENZYME DEGRADATION
ENZYME SUBSTRATE
EUKARYOTE
NONHUMAN
NUCLEOTIDE SEQUENCE
OXIDATION REDUCTION REACTION
PHOTOSYSTEM II
PROKARYOTE
PROTEIN ASSEMBLY
PROTEIN CLEAVAGE
PROTEIN LOCALIZATION
SPINACH
SYNECHOCOCCUS
THYLAKOID MEMBRANE
AMINO ACID SEQUENCE
BACTERIAL PROTEINS
BASE SEQUENCE
BLOTTING, WESTERN
DNA PRIMERS
ELECTROPHORESIS, POLYACRYLAMIDE GEL
KINETICS
MASS SPECTROMETRY
MOLECULAR SEQUENCE DATA
PROTEOLYSIS
RECOMBINANT PROTEINS
SUBCELLULAR FRACTIONS
SUBSTRATE SPECIFICITY
SYNECHOCYSTIS
THIOREDOXINS
EUKARYOTA
PROKARYOTA
SPINACIA OLERACEA
SYNECHOCYSTIS SP. PCC 6803
topic BACTERIAL PROTEIN
DEG PROTEASE RECOMBINANT HHOA
PROTEIN HHOA
PROTEIN HHOB
PROTEIN HTRA
PROTEIN PSBO
THIOREDOXIN
UNCLASSIFIED DRUG
BACTERIAL CELL
BACTERIAL STRAIN
CELL FRACTIONATION
CELLULAR DISTRIBUTION
CONTROLLED STUDY
CYTOPLASM
ENZYME DEGRADATION
ENZYME SUBSTRATE
EUKARYOTE
NONHUMAN
NUCLEOTIDE SEQUENCE
OXIDATION REDUCTION REACTION
PHOTOSYSTEM II
PROKARYOTE
PROTEIN ASSEMBLY
PROTEIN CLEAVAGE
PROTEIN LOCALIZATION
SPINACH
SYNECHOCOCCUS
THYLAKOID MEMBRANE
AMINO ACID SEQUENCE
BACTERIAL PROTEINS
BASE SEQUENCE
BLOTTING, WESTERN
DNA PRIMERS
ELECTROPHORESIS, POLYACRYLAMIDE GEL
KINETICS
MASS SPECTROMETRY
MOLECULAR SEQUENCE DATA
PROTEOLYSIS
RECOMBINANT PROTEINS
SUBCELLULAR FRACTIONS
SUBSTRATE SPECIFICITY
SYNECHOCYSTIS
THIOREDOXINS
EUKARYOTA
PROKARYOTA
SPINACIA OLERACEA
SYNECHOCYSTIS SP. PCC 6803
dc.description.none.fl_txt_mv Fil: Roberts, Irma N. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales (INBA). Buenos Aires, Argentina.
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.
description Fil: Roberts, Irma N. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales (INBA). Buenos Aires, Argentina.
publishDate 2012
dc.date.none.fl_str_mv 2012
dc.type.none.fl_str_mv article
info:eu-repo/semantics/article
publishedVersion
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 doi:10.1371/journal.pone.0045713
issn:1932-6203
http://ri.agro.uba.ar/greenstone3/library/collection/arti/document/2012Roberts
identifier_str_mv doi:10.1371/journal.pone.0045713
issn:1932-6203
url http://ri.agro.uba.ar/greenstone3/library/collection/arti/document/2012Roberts
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
openAccess
http://ri.agro.uba.ar/greenstone3/library/page/biblioteca#section4
eu_rights_str_mv openAccess
rights_invalid_str_mv openAccess
http://ri.agro.uba.ar/greenstone3/library/page/biblioteca#section4
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Plos One
Vol.7, no.9
e45713
http://www.plos.org/
reponame:FAUBA Digital (UBA-FAUBA)
instname:Universidad de Buenos Aires. Facultad de Agronomía
reponame_str FAUBA Digital (UBA-FAUBA)
collection FAUBA Digital (UBA-FAUBA)
instname_str Universidad de Buenos Aires. Facultad de Agronomía
repository.name.fl_str_mv FAUBA Digital (UBA-FAUBA) - Universidad de Buenos Aires. Facultad de Agronomía
repository.mail.fl_str_mv martino@agro.uba.ar;berasa@agro.uba.ar
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score 13.070432