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

2019-12Journal article Open access
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dc.contributor.authorKrynicka, Vendula
dc.contributor.authorGeorg, Jens
dc.contributor.authorJackson, Philip J.
dc.contributor.authorDickman, Mark J.
dc.contributor.authorHunter, C. Neil
dc.contributor.authorFutschik, Matthias
dc.contributor.authorHess, Wolfgang R.
dc.contributor.authorKomenda, Josef
dc.date.accessioned2020-07-24T10:50:46Z
dc.date.available2020-07-24T10:50:46Z
dc.date.issued2019-12
dc.description.abstractThe 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.
dc.description.sponsorshipGermany Federal Ministry of Education and Research [031L0106B]
dc.description.sponsorshipGrant Agency of the Czech RepublicGrant Agency of the Czech Republic [P501-12-G055]
dc.description.sponsorshipCzech Ministry of Education Ministry of Education, Youth & Sports - Czech Republic [LO1416]
dc.description.sponsorshipPortuguese Fundacao para a Ciencia e a Tecnologia (Foundation for Science and Technology) [PTDC/BIA-MIC/4418/2012, IF/00881/2013, UID/Multi/04326/2013]
dc.description.sponsorshipUnited Kingdom Biotechnology and Biological Sciences Research Council (BBSRC)Biotechnology and Biological Sciences Research Council (BBSRC) [BB/M012166/1, BB/M000265/1]
dc.description.sponsorshipEuropean Research CouncilEuropean Research Council (ERC) [338895]
dc.identifier.doi10.1105/tpc.19.00411
dc.identifier.issn1040-4651
dc.identifier.issn1532-298X
dc.identifier.urihttp://hdl.handle.net/10400.1/14150
dc.language.isoeng
dc.peerreviewedyes
dc.publisherAmerican Society of Plant Biologists
dc.relationThe regulation of photosynthesis in cyanobacteria: A systems biology approach
dc.subjectSignal transduction
dc.subjectPhotosystem Ii
dc.subjectEscherichia coli
dc.subjectNitrogen starvation
dc.subjectGene expression
dc.subjectProtein
dc.subjectPhosphate
dc.subjectRegulator
dc.subjectAccumulation
dc.subjectAcclimation
dc.titleDepletion of the FtsH1/3 proteolytic complex suppresses the nutrient stress response in the cyanobacterium synechocystis sp strain PCC 6803
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleThe regulation of photosynthesis in cyanobacteria: A systems biology approach
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-MIC%2F4418%2F2012/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FMulti%2F04326%2F2013/PT
oaire.citation.endPage2928
oaire.citation.issue12
oaire.citation.startPage2912
oaire.citation.titlePlant Cell
oaire.citation.volume31
oaire.fundingStream3599-PPCDT
oaire.fundingStream5876
person.familyNameFutschik
person.givenNameMatthias
person.identifier.ciencia-idA71B-AD01-3501
person.identifier.orcid0000-0002-6245-8071
person.identifier.scopus-author-id14017989400
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
rcaap.typearticle
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relation.isAuthorOfPublication.latestForDiscoveryd58f3269-c7e1-4c22-b094-5cfe6750821b
relation.isProjectOfPublication50660995-5319-4cb4-bf59-4d5a080d4f55
relation.isProjectOfPublication868b4818-3efa-4edb-9202-c464d64fd38f
relation.isProjectOfPublication.latestForDiscovery50660995-5319-4cb4-bf59-4d5a080d4f55

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