Tags

Type your tag names separated by a space and hit enter

Osmotic induction of the periplasmic trehalase in Escherichia coli K12: characterization of the treA gene promoter.
Mol Microbiol 1991; 5(3):747-55MM

Abstract

The Escherichia coli treA gene encodes an osmotically inducible periplasmic trehalase. A strain carrying a treA-lacZ transcriptional fusion was constructed. The beta-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 sigma 70 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.

Authors+Show Affiliations

Centre de Recherche de Biochiminie et Génétique Cellulaire du CNRS, Toulouse, France.No affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

1710760

Citation

Repoila, F, and C Gutierrez. "Osmotic Induction of the Periplasmic Trehalase in Escherichia Coli K12: Characterization of the treA Gene Promoter." Molecular Microbiology, vol. 5, no. 3, 1991, pp. 747-55.
Repoila F, Gutierrez C. Osmotic induction of the periplasmic trehalase in Escherichia coli K12: characterization of the treA gene promoter. Mol Microbiol. 1991;5(3):747-55.
Repoila, F., & Gutierrez, C. (1991). Osmotic induction of the periplasmic trehalase in Escherichia coli K12: characterization of the treA gene promoter. Molecular Microbiology, 5(3), pp. 747-55.
Repoila F, Gutierrez C. Osmotic Induction of the Periplasmic Trehalase in Escherichia Coli K12: Characterization of the treA Gene Promoter. Mol Microbiol. 1991;5(3):747-55. PubMed PMID: 1710760.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Osmotic induction of the periplasmic trehalase in Escherichia coli K12: characterization of the treA gene promoter. AU - Repoila,F, AU - Gutierrez,C, PY - 1991/3/1/pubmed PY - 1991/3/1/medline PY - 1991/3/1/entrez SP - 747 EP - 55 JF - Molecular microbiology JO - Mol. Microbiol. VL - 5 IS - 3 N2 - The Escherichia coli treA gene encodes an osmotically inducible periplasmic trehalase. A strain carrying a treA-lacZ transcriptional fusion was constructed. The beta-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 sigma 70 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. SN - 0950-382X UR - https://www.unboundmedicine.com/medline/citation/1710760/Osmotic_induction_of_the_periplasmic_trehalase_in_Escherichia_coli_K12:_characterization_of_the_treA_gene_promoter_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0950-382X&date=1991&volume=5&issue=3&spage=747 DB - PRIME DP - Unbound Medicine ER -