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
- Institución
- Universidad de Buenos Aires. Facultad de Agronomía
- OAI Identificador
- snrd:2012Roberts
Ver los metadatos del registro completo
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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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1844618854484934656 |
score |
13.070432 |