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Tetracycline alters gene expression in Salmonella strains that harbor the Tn 10 transposon
Author(s) -
Hüttener M.,
Prieto A.,
Aznar S.,
Dietrich M.,
Paytubi S.,
Juárez A.
Publication year - 2018
Publication title -
environmental microbiology reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.229
H-Index - 69
ISSN - 1758-2229
DOI - 10.1111/1758-2229.12621
Subject(s) - regulon , tn10 , biology , salmonella enterica , heat shock protein , transposable element , periplasmic space , repressor , plasmid , operon , gene , chaperone (clinical) , gene expression , microbiology and biotechnology , genetics , escherichia coli , medicine , pathology , genome
Summary In this report, we show that bacterial plasmids that harbor the Tn 10 transposon (i.e., the IncHI1 plasmid R27) modify expression of different Salmonella regulons responding to the presence of tetracycline (Tc) in the medium. By using as a model the Tc‐dependent upregulation of the ibpAB operon (which belongs to the heat shock regulon), we have identified Tn 10 ‐ tetA (coding for a Tc efflux pump) and adjacent tetC sequences as required for ibpAB upregulation. Characterization of transcripts in the tetAC region showed that tetA transcription can continue into tetC sequences, generating a long 3′UTR sequence, which can protect transcripts from RNA processing, thus increasing the expression of TetA protein. In the presence of Tc, the DnaK and IbpA chaperones are overexpressed and translocated to the periplasm and to the membrane fraction respectively. DnaK targeting unfolded proteins is known to induce heat shock by avoiding RpoH proteolysis. We correlate expression levels of Tn 10‐ encoded TetA protein with heat shock induction in Salmonella , likely because TetA activity compromises protein secretion.