A1 Refereed original research article in a scientific journal
FtsH protease is required for induction of inorganic carbon acquisition complexes in Synechocystis sp PCC 6803
Authors: Zhang PP, Sicora CI, Vorontsova N, Allahverdlyeva Y, Battchikova N, Nixon PJ, Aro EM
Publisher: BLACKWELL PUBLISHING
Publication year: 2007
Journal:: Molecular Microbiology
Journal name in source: MOLECULAR MICROBIOLOGY
Journal acronym: MOL MICROBIOL
Volume: 65
Issue: 3
First page : 728
Last page: 740
Number of pages: 13
ISSN: 0950-382X
DOI: https://doi.org/10.1111/j.1365-2958.2007.05822.x
Abstract
Cyanobacteria possess a complex C02-concentrating mechanism (CCM), which is induced by low inorganic carbon conditions. To investigate the involvement of proteases in the processes of induction and degradation of the CCM complexes, we studied the FtsH2 (Delta SIr0228) and Deg-G (Delta SIr1204/Delta SII1679/Delta SII1427) protease mutants of Synechocystis sp. PCC 6803. WT and protease mutant cells were grown under high CO2 and then shifted to low CO2, followed by a proteome analysis of the membrane protein complexes. Interestingly, in the FtsH2 protease mutant, inducible CCM complexes were not detected upon shift to low CO2, whereas the Deg-G mutant behaved like WT Also the transcripts of the inducible CCM genes and their regulator ndhR failed to accumulate upon shift of FtsH2 mutant cells from high to low CO2, indicating that the regulation by the FtsH2 protease is upstream of NdhR. Moreover, functional photosynthesis was shown a prerequisite for induction of CCM in WT at low CO2, possibly via generation of oxidative stress, which was shown here to enhance the expression of inducible CCM genes even at high CO2 conditions. Once synthesized, the CCM complexes were not subject to proteolytic degradation, even when dispensable upon a shift of cells to high CO2.
Cyanobacteria possess a complex C02-concentrating mechanism (CCM), which is induced by low inorganic carbon conditions. To investigate the involvement of proteases in the processes of induction and degradation of the CCM complexes, we studied the FtsH2 (Delta SIr0228) and Deg-G (Delta SIr1204/Delta SII1679/Delta SII1427) protease mutants of Synechocystis sp. PCC 6803. WT and protease mutant cells were grown under high CO2 and then shifted to low CO2, followed by a proteome analysis of the membrane protein complexes. Interestingly, in the FtsH2 protease mutant, inducible CCM complexes were not detected upon shift to low CO2, whereas the Deg-G mutant behaved like WT Also the transcripts of the inducible CCM genes and their regulator ndhR failed to accumulate upon shift of FtsH2 mutant cells from high to low CO2, indicating that the regulation by the FtsH2 protease is upstream of NdhR. Moreover, functional photosynthesis was shown a prerequisite for induction of CCM in WT at low CO2, possibly via generation of oxidative stress, which was shown here to enhance the expression of inducible CCM genes even at high CO2 conditions. Once synthesized, the CCM complexes were not subject to proteolytic degradation, even when dispensable upon a shift of cells to high CO2.
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