Osmotic induction of gene osmC expression in Escherichia coli K12

Gutierrez, Claude; Devedjian, Jean Christophe

doi:10.1016/0022-2836(91)90366-e

Cited by 96 publications

(96 citation statements)

References 50 publications

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“…A similar analysis of E. coli osmC mutants failed to detect any physiological alterations (Gutierrez & Devedjian, 1991). The distinct phenotypes of the ohr and osmC mutants, and the inability of the osmC gene to complement the ohr mutant, support the idea that these genes play different roles in the cell.…”

Section: Ohr and Osmc Homologues Have Different Physiological Rolesmentioning

confidence: 67%

“…Thus, the patterns of ohr and osmC expression in P. aeruginosa and D. radiodurans are consistent with the known regulation of X. campestris pv. phaseoli ohr (Mongkolsuk et al, 1998a) and E. coli osmC (Gutierrez & Devedjian, 1991). The ohr and osmC mRNAs in both bacterial species were each approximately 0n7 kb in length, indicating that these genes are transcribed as monocistronic mRNAs.…”

Section: Ohr and Osmc Homologues Have Different Physiological Rolesmentioning

confidence: 98%

“…This unusual pattern of induction distinguishes ohr from other known oxidative stress genes. Analysis of Ohr primary structure shows that it has homology to proteins with unknown functions from both Gram-positive and Gram-negative bacteria, and that it has moderate homology to an osmotically inducible protein (OsmC) from Escherichia coli (Gutierrez & Devedjian, 1991).…”

Section: Abbreviationsmentioning

confidence: 99%

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Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression

et al. 2001

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Xanthomonas campestris Ohr (a protein involved in organic peroxide protection) and Escherichia coli OsmC (an osmotically inducible protein of unknown function) are related proteins. Database searches and phylogenetic analyses reveal that Ohr and OsmC homologues cluster into two related subfamilies of proteins widely distributed in both Gram-negative and Grampositive bacteria. To determine if these two subfamilies are functionally distinct, ohr and osmC in Pseudomonas aeruginosa (a bacterium with one representative from each subfamily) were analysed. Only ohr mutants are hypersensitive to organic peroxide, and this phenotype can be restored by complementation with ohr but not osmC. In addition, expression of ohr was highly induced only by organic peroxides, and not by other oxidants or stresses. In contrast, osmC was induced by ethanol and osmotic stress. A similar pattern of regulation was observed for Ohr and OsmC homologues in the Gram-positive bacterium Deinococcus radiodurans, though uninduced expression was much higher and induction lower in this species. These data clearly support the conclusion that Ohr and OsmC define two functionally distinct subfamilies with distinct patterns of regulation.

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Section: Ohr and Osmc Homologues Have Different Physiological Rolesmentioning

confidence: 67%

Section: Ohr and Osmc Homologues Have Different Physiological Rolesmentioning

confidence: 98%

Section: Abbreviationsmentioning

confidence: 99%

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Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression

et al. 2001

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“…These proteins were initially identified as part of the bacterial response to osmotic stress (14). On the basis of sequence analysis, Atichartpongkul et al (10) proposed Ohr and OsmC homologues as two protein subfamilies.…”

mentioning

confidence: 99%

Ohr (Organic Hydroperoxide Resistance Protein) Possesses a Previously Undescribed Activity, Lipoyl-dependent Peroxidase

Cussiol

Alegria

Szweda

et al. 2010

Journal of Biological Chemistry

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The Ohr (organic hydroperoxide resistance) family of 15-kDa Cys-based, thiol-dependent peroxidases is central to the bacterial response to stress induced by organic hydroperoxides but not by hydrogen peroxide. Ohr has a unique three-dimensional structure and requires dithiols, but not monothiols, to support its activity. However, the physiological reducing system of Ohr has not yet been identified. Here we show that lipoylated enzymes present in the bacterial extracts of Xylella fastidiosa interacted physically and functionally with this Cys-based peroxidase, whereas thioredoxin and glutathione systems failed to support Ohr peroxidase activity. Furthermore, we could reconstitute in vitro three lipoyl-dependent systems as the Ohr physiological reducing systems. We also showed that OsmC from Escherichia coli, an orthologue of Ohr from Xylella fastidiosa, is specifically reduced by lipoyl-dependent systems. These results represent the first description of a Cys-based peroxidase that is directly reduced by lipoylated enzymes.

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“…osmB, which encodes an outer membrane lipoprotein (20), is induced by hyperosmotic stress and by stationary growth phase (19), but its expression in an in vitro transcription-translation system does not seem to be K+ stimulated (our unpublished data). osmC (15) is K+ stimulated in vitro in a manner analogous to proU (38), but its expression is also growth phase dependent. Because OsmY appeared to have induction kinetics very similar to those of the periplasmic component of the proU operon, osmY seemed a likely candidate for an analogous mechanism of osmotic regulation.…”

mentioning

confidence: 99%

osmY, a new hyperosmotically inducible gene, encodes a periplasmic protein in Escherichia coli

1992

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A new osmotically inducible gene in Escherichia coli, osmY, was induced 8- to 10-fold by hyperosmotic stress and 2- to 3-fold by growth in complex medium. The osmY gene product is a periplasmic protein which migrates with an apparent molecular mass of 22 kDa on sodium dodecyl sulfate-polyacrylamide gels. A genetic fusion to osmY was mapped to 99.3 min on the E. coli chromosome. The gene was cloned and sequenced, and an open reading frame was identified. The open reading frame encoded a precursor protein with a calculated molecular weight of 21,090 and a mature protein of 18,150 following signal peptide cleavage. Sequencing of the periplasmic OsmY protein confirmed the open reading frame and defined the signal peptide cleavage site as Ala-Glu. A mutation caused by the osmY::TnphoA genetic fusion resulted in slightly increased sensitivity to hyperosmotic stress.

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Osmotic induction of gene osmC expression in Escherichia coli K12

Cited by 96 publications

References 50 publications

Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression

Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression

Ohr (Organic Hydroperoxide Resistance Protein) Possesses a Previously Undescribed Activity, Lipoyl-dependent Peroxidase

osmY, a new hyperosmotically inducible gene, encodes a periplasmic protein in Escherichia coli

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