Depletion of the FtsH1/3 proteolytic complex suppresses the nutrient stress response in the cyanobacterium synechocystis sp strain PCC 6803

Detalhes bibliográficos
Autor(a) principal: Krynicka, Vendula
Data de Publicação: 2019
Outros Autores: Georg, Jens, Jackson, Philip J., Dickman, Mark J., Hunter, C. Neil, Futschik, Matthias, Hess, Wolfgang R., Komenda, Josef
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.1/14150
Resumo: The membrane-embedded FtsH proteases found in bacteria, chloroplasts, and mitochondria are involved in diverse cellular processes including protein quality control and regulation. The genome of the model cyanobacterium Synechocystis sp PCC 6803 encodes four FtsH homologs designated FtsH1 to FtsH4. The FtsH3 homolog is present in two hetero-oligomeric complexes: FtsH2/3, which is responsible for photosystem II quality control, and the essential FtsH1/3 complex, which helps maintain Fe homeostasis by regulating the level of the transcription factor Fur. To gain a more comprehensive insight into the physiological roles of FtsH hetero-complexes, we performed genome-wide expression profiling and global proteomic analyses of Synechocystis mutants conditionally depleted of FtsH3 or FtsH1 grown under various nutrient conditions. We show that the lack of FtsH1/3 leads to a drastic reduction in the transcriptional response to nutrient stress of not only Fur but also the Pho, NdhR, and NtcA regulons. In addition, this effect is accompanied by the accumulation of the respective transcription factors. Thus, the FtsH1/3 complex is of critical importance for acclimation to iron, phosphate, carbon, and nitrogen starvation in Synechocystis.
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spelling Depletion of the FtsH1/3 proteolytic complex suppresses the nutrient stress response in the cyanobacterium synechocystis sp strain PCC 6803Signal transductionPhotosystem IiEscherichia coliNitrogen starvationGene expressionProteinPhosphateRegulatorAccumulationAcclimationThe membrane-embedded FtsH proteases found in bacteria, chloroplasts, and mitochondria are involved in diverse cellular processes including protein quality control and regulation. The genome of the model cyanobacterium Synechocystis sp PCC 6803 encodes four FtsH homologs designated FtsH1 to FtsH4. The FtsH3 homolog is present in two hetero-oligomeric complexes: FtsH2/3, which is responsible for photosystem II quality control, and the essential FtsH1/3 complex, which helps maintain Fe homeostasis by regulating the level of the transcription factor Fur. To gain a more comprehensive insight into the physiological roles of FtsH hetero-complexes, we performed genome-wide expression profiling and global proteomic analyses of Synechocystis mutants conditionally depleted of FtsH3 or FtsH1 grown under various nutrient conditions. We show that the lack of FtsH1/3 leads to a drastic reduction in the transcriptional response to nutrient stress of not only Fur but also the Pho, NdhR, and NtcA regulons. In addition, this effect is accompanied by the accumulation of the respective transcription factors. Thus, the FtsH1/3 complex is of critical importance for acclimation to iron, phosphate, carbon, and nitrogen starvation in Synechocystis.Germany Federal Ministry of Education and Research [031L0106B]Grant Agency of the Czech RepublicGrant Agency of the Czech Republic [P501-12-G055]Czech Ministry of Education Ministry of Education, Youth & Sports - Czech Republic [LO1416]Portuguese Fundacao para a Ciencia e a Tecnologia (Foundation for Science and Technology) [PTDC/BIA-MIC/4418/2012, IF/00881/2013, UID/Multi/04326/2013]United Kingdom Biotechnology and Biological Sciences Research Council (BBSRC)Biotechnology and Biological Sciences Research Council (BBSRC) [BB/M012166/1, BB/M000265/1]European Research CouncilEuropean Research Council (ERC) [338895]American Society of Plant BiologistsSapientiaKrynicka, VendulaGeorg, JensJackson, Philip J.Dickman, Mark J.Hunter, C. NeilFutschik, MatthiasHess, Wolfgang R.Komenda, Josef2020-07-24T10:50:46Z2019-122019-12-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/14150eng1040-465110.1105/tpc.19.00411info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-24T10:26:24Zoai:sapientia.ualg.pt:10400.1/14150Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:05:12.225534Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Depletion of the FtsH1/3 proteolytic complex suppresses the nutrient stress response in the cyanobacterium synechocystis sp strain PCC 6803
title Depletion of the FtsH1/3 proteolytic complex suppresses the nutrient stress response in the cyanobacterium synechocystis sp strain PCC 6803
spellingShingle Depletion of the FtsH1/3 proteolytic complex suppresses the nutrient stress response in the cyanobacterium synechocystis sp strain PCC 6803
Krynicka, Vendula
Signal transduction
Photosystem Ii
Escherichia coli
Nitrogen starvation
Gene expression
Protein
Phosphate
Regulator
Accumulation
Acclimation
title_short Depletion of the FtsH1/3 proteolytic complex suppresses the nutrient stress response in the cyanobacterium synechocystis sp strain PCC 6803
title_full Depletion of the FtsH1/3 proteolytic complex suppresses the nutrient stress response in the cyanobacterium synechocystis sp strain PCC 6803
title_fullStr Depletion of the FtsH1/3 proteolytic complex suppresses the nutrient stress response in the cyanobacterium synechocystis sp strain PCC 6803
title_full_unstemmed Depletion of the FtsH1/3 proteolytic complex suppresses the nutrient stress response in the cyanobacterium synechocystis sp strain PCC 6803
title_sort Depletion of the FtsH1/3 proteolytic complex suppresses the nutrient stress response in the cyanobacterium synechocystis sp strain PCC 6803
author Krynicka, Vendula
author_facet Krynicka, Vendula
Georg, Jens
Jackson, Philip J.
Dickman, Mark J.
Hunter, C. Neil
Futschik, Matthias
Hess, Wolfgang R.
Komenda, Josef
author_role author
author2 Georg, Jens
Jackson, Philip J.
Dickman, Mark J.
Hunter, C. Neil
Futschik, Matthias
Hess, Wolfgang R.
Komenda, Josef
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Sapientia
dc.contributor.author.fl_str_mv Krynicka, Vendula
Georg, Jens
Jackson, Philip J.
Dickman, Mark J.
Hunter, C. Neil
Futschik, Matthias
Hess, Wolfgang R.
Komenda, Josef
dc.subject.por.fl_str_mv Signal transduction
Photosystem Ii
Escherichia coli
Nitrogen starvation
Gene expression
Protein
Phosphate
Regulator
Accumulation
Acclimation
topic Signal transduction
Photosystem Ii
Escherichia coli
Nitrogen starvation
Gene expression
Protein
Phosphate
Regulator
Accumulation
Acclimation
description The membrane-embedded FtsH proteases found in bacteria, chloroplasts, and mitochondria are involved in diverse cellular processes including protein quality control and regulation. The genome of the model cyanobacterium Synechocystis sp PCC 6803 encodes four FtsH homologs designated FtsH1 to FtsH4. The FtsH3 homolog is present in two hetero-oligomeric complexes: FtsH2/3, which is responsible for photosystem II quality control, and the essential FtsH1/3 complex, which helps maintain Fe homeostasis by regulating the level of the transcription factor Fur. To gain a more comprehensive insight into the physiological roles of FtsH hetero-complexes, we performed genome-wide expression profiling and global proteomic analyses of Synechocystis mutants conditionally depleted of FtsH3 or FtsH1 grown under various nutrient conditions. We show that the lack of FtsH1/3 leads to a drastic reduction in the transcriptional response to nutrient stress of not only Fur but also the Pho, NdhR, and NtcA regulons. In addition, this effect is accompanied by the accumulation of the respective transcription factors. Thus, the FtsH1/3 complex is of critical importance for acclimation to iron, phosphate, carbon, and nitrogen starvation in Synechocystis.
publishDate 2019
dc.date.none.fl_str_mv 2019-12
2019-12-01T00:00:00Z
2020-07-24T10:50:46Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.1/14150
url http://hdl.handle.net/10400.1/14150
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1040-4651
10.1105/tpc.19.00411
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Society of Plant Biologists
publisher.none.fl_str_mv American Society of Plant Biologists
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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