FtsH protease is required for induction of inorganic carbon acquisition complexes in Synechocystis sp. PCC 6803
Cyanobacteria possess a complex CO₂-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 (ΔSlr0228) and Deg-G (ΔSlr1204/ΔSll1679/ΔSll142...
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| Published in | Molecular microbiology Vol. 65; no. 3; pp. 728 - 740 |
|---|---|
| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford, UK
Oxford, UK : Blackwell Publishing Ltd
01.08.2007
Blackwell Publishing Ltd Blackwell Science |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0950-382X 1365-2958 |
| DOI | 10.1111/j.1365-2958.2007.05822.x |
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| Abstract | Cyanobacteria possess a complex CO₂-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 (ΔSlr0228) and Deg-G (ΔSlr1204/ΔSll1679/ΔSll1427) 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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| AbstractList | Cyanobacteria possess a complex CO(2)-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 (DeltaSlr0228) and Deg-G (DeltaSlr1204/DeltaSll1679/DeltaSll1427) protease mutants of Synechocystis sp. PCC 6803. WT and protease mutant cells were grown under high CO(2) and then shifted to low CO(2), 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 CO(2), 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 CO(2), 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 CO(2), possibly via generation of oxidative stress, which was shown here to enhance the expression of inducible CCM genes even at high CO(2) conditions. Once synthesized, the CCM complexes were not subject to proteolytic degradation, even when dispensable upon a shift of cells to high CO(2).Cyanobacteria possess a complex CO(2)-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 (DeltaSlr0228) and Deg-G (DeltaSlr1204/DeltaSll1679/DeltaSll1427) protease mutants of Synechocystis sp. PCC 6803. WT and protease mutant cells were grown under high CO(2) and then shifted to low CO(2), 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 CO(2), 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 CO(2), 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 CO(2), possibly via generation of oxidative stress, which was shown here to enhance the expression of inducible CCM genes even at high CO(2) conditions. Once synthesized, the CCM complexes were not subject to proteolytic degradation, even when dispensable upon a shift of cells to high CO(2). Cyanobacteria possess a complex CO₂-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 (ΔSlr0228) and Deg-G (ΔSlr1204/ΔSll1679/ΔSll1427) 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 ...-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 (...) and Deg-G (...) protease mutants of Synechocystis sp. PCC 6803. WT and protease mutant cells were grown under high ... and then shifted to low ..., 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 ..., 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 ..., 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 ..., possibly via generation of oxidative stress, which was shown here to enhance the expression of inducible CCM genes even at high ... conditions. Once synthesized, the CCM complexes were not subject to proteolytic degradation, even when dispensable upon a shift of cells to high ... (ProQuest-CSA LLC: ... denotes formulae/symbols omitted.) Summary Cyanobacteria possess a complex CO2‐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 (ΔSlr0228) and Deg‐G (ΔSlr1204/ΔSll1679/ΔSll1427) 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 CO(2)-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 (DeltaSlr0228) and Deg-G (DeltaSlr1204/DeltaSll1679/DeltaSll1427) protease mutants of Synechocystis sp. PCC 6803. WT and protease mutant cells were grown under high CO(2) and then shifted to low CO(2), 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 CO(2), 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 CO(2), 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 CO(2), possibly via generation of oxidative stress, which was shown here to enhance the expression of inducible CCM genes even at high CO(2) conditions. Once synthesized, the CCM complexes were not subject to proteolytic degradation, even when dispensable upon a shift of cells to high CO(2). Cyanobacteria possess a complex CO(2)-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 (∆Slr0228) and Deg-G (∆Slr1204/∆Sll1679/∆Sll1427) protease mutants of Synechocystis sp. PCC 6803. WT and protease mutant cells were grown under high CO(2) and then shifted to low CO(2), 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 CO(2), 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 CO(2), 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 CO(2), possibly via generation of oxidative stress, which was shown here to enhance the expression of inducible CCM genes even at high CO(2) conditions. Once synthesized, the CCM complexes were not subject to proteolytic degradation, even when dispensable upon a shift of cells to high CO(2). Cyanobacteria possess a complex CO 2 ‐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 (ΔSlr0228) and Deg‐G (ΔSlr1204/ΔSll1679/ΔSll1427) protease mutants of Synechocystis sp. PCC 6803. WT and protease mutant cells were grown under high CO 2 and then shifted to low CO 2 , 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 CO 2 , 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 CO 2 , 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 CO 2 , possibly via generation of oxidative stress, which was shown here to enhance the expression of inducible CCM genes even at high CO 2 conditions. Once synthesized, the CCM complexes were not subject to proteolytic degradation, even when dispensable upon a shift of cells to high CO 2 . |
| Author | Allahverdiyeva, Yagut Battchikova, Natalia Vorontsova, Natalia Nixon, Peter J Aro, Eva-Mari Sicora, Cosmin I Zhang, Pengpeng |
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| Keywords | Peptidases Bacteria Hydrolases Synechocystis Enzyme Cyanobacteria |
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| Snippet | Cyanobacteria possess a complex CO₂-concentrating mechanism (CCM), which is induced by low inorganic carbon conditions. To investigate the involvement of... Summary Cyanobacteria possess a complex CO2‐concentrating mechanism (CCM), which is induced by low inorganic carbon conditions. To investigate the involvement... Cyanobacteria possess a complex CO 2 ‐concentrating mechanism (CCM), which is induced by low inorganic carbon conditions. To investigate the involvement of... Cyanobacteria possess a complex CO(2)-concentrating mechanism (CCM), which is induced by low inorganic carbon conditions. To investigate the involvement of... Cyanobacteria possess a complex ...-concentrating mechanism (CCM), which is induced by low inorganic carbon conditions. To investigate the involvement of... |
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| SubjectTerms | Autoradiography Bacteria Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biochemistry Biological and medical sciences Carbon Compounds, Inorganic - metabolism Carbon dioxide Carbon Dioxide - metabolism Diuron - pharmacology Environment Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial - drug effects Genes, Bacterial Inorganic carbon Microbiology Miscellaneous Models, Biological Mutants Mutation - genetics Oxidative stress Paraquat - pharmacology Photosynthesis Proteases Protein Biosynthesis - drug effects Proteome - metabolism RNA, Messenger - genetics RNA, Messenger - metabolism Synechocystis - cytology Synechocystis - drug effects Synechocystis - enzymology Synechocystis - genetics |
| Title | FtsH protease is required for induction of inorganic carbon acquisition complexes in Synechocystis sp. PCC 6803 |
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