Osmotic induction of the periplasmic trehalase in Escherichia coli K12: characterization of the treA gene promoter

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Abstract
The Escherichia coli treA gene encodes an osmotically inducible periplasmic trehalase. A strain carrying a treA–lacZ transcriptional fusion was constructed. The β-galactosidase activity produced in this strain growing exponentially in a medium of high osmotic pressure was 10-fold higher than that produced in a medium of low osmotic pressure, demonstrating that treA transcription is osmotically inducible. treA transcriptional induction depends neither on the presence of trehalase itself nor on the synthesis of cytoplasmic trehalose which occurs in response to osmotic stress in wild-type E. coli strains. The treA promoter was identified by S1 nuclease protection. Deletion analysis demonstrated that sequences sufficient for the osmotic induction lie downstream from nucleotide –40 with respect to the transcription start. Transcription initiation at treAp required the presence of a functional σ70 subunit of RNA polymerase. treA expression was increased in the presence of a mutation in osmZ, which was previously identified as leading to a partially constitutive expression of the osmotically inducible proU operon.