ArticleBMC microbiology2007
A proteomic study of Corynebacterium glutamicum AAA+ protease FtsH.
Article in BMC microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Review of the Proteomics and Metabolic Properties ofMicroorganisms · 2024Review
- Degradation Mechanism of AAA+ Proteases and Regulation ofBiomolecules · 2022Review
- Cellular and Extracellular Proteome of the Animal PathogenProteomes · 2020Article
- Metallopeptidases of Toxoplasma gondii: in silico identification and gene expression.Parasite (Paris, France) · 2018Article
- Multi-Omics and Targeted Approaches to Determine the Role of Cellular Proteases inFrontiers in microbiology · 2018Article
- Rewiring of the FtsH regulatory network by a single nucleotide change in saeS of Staphylococcus aureus.Scientific reports · 2017Article
- The pupylation machinery is involved in iron homeostasis by targeting the iron storage protein ferritin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Role of Corynebacterium glutamicum sprA encoding a serine protease in glxR-mediated global gene regulation.PloS one · 2014Article
- Precipitation of iron on the surface of Leptospira interrogans is associated with mutation of the stress response metalloprotease HtpX.Applied and environmental microbiology · 2013Article
- ClpL is required for folding of CtsR in Streptococcus mutans.Journal of bacteriology · 2013Article
- The Lactobacillus plantarum ftsH gene is a novel member of the CtsR stress response regulon.Journal of bacteriology · 2009Article
- Response of the cytoplasmic and membrane proteome of Corynebacterium glutamicum ATCC 13032 to pH changes.BMC microbiology · 2008Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe influence of the membrane-bound AAA+ protease FtsH on membrane and cytoplasmic proteins of Corynebacterium glutamicum was investigated in this study. For the analysis of the membrane fraction, anion exchange chromatography was combined with SDS-PAGE, while the cytoplasmic protein fraction was studied by conventional two-dimensional gel electrophoresis.
resultsIn contrast to the situation in other bacteria, deletion of C. glutamicum ftsH has no significant effect on growth in standard minimal medium or response to heat or osmotic stress. On the proteome level, deletion of the ftsH gene resulted in a strong increase of ten cytoplasmic and membrane proteins, namely biotin carboxylase/biotin carboxyl carrier protein (accBC), glyceraldehyde-3-phosphate dehydrogenase (gap), homocysteine methyltransferase (metE), malate synthase (aceB), isocitrate lyase (aceA), a conserved hypothetical protein (NCgl1985), succinate dehydrogenase A (sdhA), succinate dehydrogenase B (sdhB), succinate dehydrogenase CD (sdhCD), and glutamate binding protein (gluB), while 38 cytoplasmic and membrane-associated proteins showed a decreased abundance. The decreasing amount of succinate dehydrogenase A (sdhA) in the cytoplasmic fraction of the ftsH mutant compared to the wild type and its increasing abundance in the membrane fraction indicates that FtsH might be involved in the cleavage of a membrane anchor of this membrane-associated protein and by this changes its localization.
conclusionThe data obtained hint to an involvement of C. glutamicum FtsH protease mainly in regulation of energy and carbon metabolism, while the protease is not involved in stress response, as found in other bacteria.
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