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Depletion of the FtsH1/3 Proteolytic Complex Suppresses the Nutrient Stress Response in the Cyanobacterium Synechocystis sp strain PCC 6803
V. Krynická, J. Georg, PJ. Jackson, MJ. Dickman, CN. Hunter, ME. Futschik, WR. Hess, J. Komenda,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
Grantová podpora
BB/M012166/1
Biotechnology and Biological Sciences Research Council - United Kingdom
BB/M000265/1
Biotechnology and Biological Sciences Research Council - United Kingdom
NLK
Free Medical Journals
od 1989 do Před 1 rokem
Freely Accessible Science Journals
od 1989 do Před 12 měsíci
Open Access Digital Library
od 1989-01-01
PubMed
31615847
DOI
10.1105/tpc.19.00411
Knihovny.cz E-zdroje
- MeSH
- aklimatizace genetika MeSH
- bakteriální proteiny genetika metabolismus MeSH
- dusík nedostatek metabolismus MeSH
- exprese genu MeSH
- fosfáty nedostatek metabolismus MeSH
- fosforylace MeSH
- fotosystém II - proteinový komplex chemie genetika metabolismus MeSH
- metaloproteasy genetika metabolismus MeSH
- mutace MeSH
- proteiny vázající fosfáty genetika metabolismus MeSH
- proteolýza MeSH
- proteom genetika metabolismus MeSH
- proteomika MeSH
- regulace genové exprese u bakterií genetika MeSH
- regulon genetika MeSH
- represorové proteiny genetika metabolismus MeSH
- ribozomální proteiny genetika metabolismus MeSH
- Synechocystis enzymologie metabolismus MeSH
- transkripční faktory genetika metabolismus MeSH
- uhlík nedostatek metabolismus MeSH
- živiny nedostatek metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
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.plantcell;31/12/2912/FX1F1fx1.
Citace poskytuje Crossref.org
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- $a 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.plantcell;31/12/2912/FX1F1fx1.
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