ArticleMolecular & cellular proteomics : MCP2008
Overproduction or absence of the periplasmic protease DegP severely compromises bacterial growth in the absence of the dithiol: disulfide oxidoreductase DsbA.
Article in Molecular & cellular proteomics : MCP, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- The Periplasmic Oxidoreductase DsbA Is Required for Virulence of the PhytopathogenInternational journal of molecular sciences · 2022Article
- Comparative differential cuproproteomes of Rhodobacter capsulatus reveal novel copper homeostasis related proteins.Metallomics : integrated biometal science · 2020Article
- Absence of Thiol-Disulfide Oxidoreductase DsbA ImpairsFrontiers in microbiology · 2017Article
- Tracking the sources of blood meals of parasitic arthropods using shotgun proteomics and unidentified tandem mass spectral libraries.Nature protocols · 2014Article
- Intermonomer electron transfer between the b hemes of heterodimeric cytochrome bc(1).Biochemistry · 2013Article
- Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response.Cellular and molecular life sciences : CMLS · 2013Review
- Missense mutations in cytochrome c maturation genes provide new insights into Rhodobacter capsulatus cbb3-type cytochrome c oxidase biogenesis.Journal of bacteriology · 2013Article
- Identifying sources of tick blood meals using unidentified tandem mass spectral libraries.Nature communications · 2013Article
- The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb₃-type cytochrome oxidase in Rhodobacter capsulatus.Biochimica et biophysica acta · 2012Article
- N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.Journal of bacteriology · 2012Article
- Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatus.Biochimica et biophysica acta · 2012Review
- OspC is potent plasminogen receptor on surface of Borrelia burgdorferi.The Journal of biological chemistry · 2012Article
- Article
- Loss of a conserved tyrosine residue of cytochrome b induces reactive oxygen species production by cytochrome bc1.The Journal of biological chemistry · 2011Article
- Vibrio cholerae anaerobic induction of virulence gene expression is controlled by thiol-based switches of virulence regulator AphB.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- A glimpse into the proteome of phototrophic bacterium Rhodobacter capsulatus.Advances in experimental medicine and biology · 2010Article
- Compensatory thio-redox interactions between DsbA, CcdA and CcmG unveil the apocytochrome c holdase role of CcmG during cytochrome c maturation.Molecular microbiology · 2008Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
Facultative phototrophic bacterium Rhodobacter capsulatus DsbA-null mutants are proficient in photosynthesis but are defective in respiration especially in enriched growth medium at 35 degrees C. They also exhibit severe pleiotropic phenotypes extending from motility defects to osmofragility and oxidative stresses. In this work, using a combined proteomics and molecular genetics approach, we demonstrated that the respiratory defect of R. capsulatus DsbA-null mutants originates from the overproduction of the periplasmic protease DegP, which renders them temperature-sensitive for growth. The DsbA-null mutants reverted frequently to overcome this growth defect by decreasing, but not completely eliminating, their DegP activity. In agreement with these findings, we showed that overproduction of DegP abolishes the newly restored respiratory growth ability of the revertants in all growth media. Structural localizations of the reversion mutations in DegP revealed the regions and amino acids that are important for its protease-chaperone activity. Remarkably although R. capsulatus DsbA-null or DegP-null mutants were viable, DegP-null DsbA-null double mutants were lethal at all growth temperatures. This is unlike Escherichia coli, and it indicates that in the absence of DsbA some DegP activity is required for survival of R. capsulatus. Absence of a DegQ protease homologue in some bacteria together with major structural variations among the DegP homologues, including a critical disulfide bond-bearing region, correlates well with the differences seen between various species like R. capsulatus and E. coli. Our findings illustrate the occurrence of two related but distinct periplasmic protease families in bacterial species.
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