ArticleJournal of bacteriology1999
Providencia stuartii genes activated by cell-to-cell signaling and identification of a gene required for production or activity of an extracellular factor.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 66 citations in OpenAlex.
- Flipping the switch: dynamic modulation of membrane transporter activity in bacteria.Microbiology (Reading, England) · 2023Review
- Review
- Proteolysis inside the membrane is a rate-governed reaction not driven by substrate affinity.Cell · 2013Article
- Conformational change in rhomboid protease GlpG induced by inhibitor binding to its S' subsites.Biochemistry · 2012Article
- Rhomboids of Mycobacteria: characterization using an aarA mutant of Providencia stuartii and gene deletion in Mycobacterium smegmatis.PloS one · 2012Article
- The rhomboid protease family: a decade of progress on function and mechanism.Genome biology · 2011Review
- Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms.Nature reviews. Microbiology · 2009Review
- Soluble oligomers of the intramembrane serine protease YqgP are catalytically active in the absence of detergents.Biochemistry · 2008Article
- Core principles of intramembrane proteolysis: comparison of rhomboid and site-2 family proteases.Current opinion in structural biology · 2008Review
- Inter-kingdom signalling: communication between bacteria and their hosts.Nature reviews. Microbiology · 2008Review
- Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by activating TatA of the twin-arginine translocase.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Functional characterization of Escherichia coli GlpG and additional rhomboid proteins using an aarA mutant of Providencia stuartii.Journal of bacteriology · 2006Article
- Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Role of CysE in production of an extracellular signaling molecule in Providencia stuartii and Escherichia coli: loss of CysE enhances biofilm formation in Escherichia coli.Journal of bacteriology · 2004Article
- BofA protein inhibits intramembrane proteolysis of pro-sigmaK in an intercompartmental signaling pathway during Bacillus subtilis sporulation.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Expression of a novel gene, gluP, is essential for normal Bacillus subtilis cell division and contributes to glucose export.BMC microbiology · 2004Article
- Interspecies communication in bacteria.The Journal of clinical investigation · 2003Review
- The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers.Genome biology · 2003Article
- A fly's eye view of EGF receptor signalling.The EMBO journal · 2002Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
By utilizing reporter transposons, five Providencia stuartii genes that are activated by the accumulation of self-produced extracellular signals have been identified. These genes have been designated cma for conditioned medium activated. The presence of conditioned medium from stationary-phase cultures grown in rich media resulted in the premature activation of each gene in cells at early log phase, with activation values ranging from 6- to 26-fold. Preparation of conditioned medium from an M9 salts medium and fractionation by gel filtration chromatography resulted in fractions within the included volume which activated three of the cma fusions. In addition, depending on the reporter fusion, peak activity was found in different fractions. The partially purified factors activated in a dose-dependent manner. Characterization of the factors activating the cma fusions indicated that they were stable to heat, alkali, and acid. Furthermore, for each cma fusion, factor activity was not reproduced by the addition of homoserine lactone, homocysteine thiolactone, pyruvate, Casamino Acids, or alpha-ketoglutarate. The identities of three cma genes have been determined and revealed physiological roles in amino acid biosynthesis and nutrient import. To begin to address the pathways for production of or response to the extracellular factors, we have identified a locus, aarA, that is required for the activation of four cma fusions. The AarA product was required for factor activity in extracellular supernatants, indicating a possible role in biosynthesis or export.
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