The ArsR protein is a trans‐acting regulatory protein
- 1 June 1991
- journal article
- Published by Wiley in Molecular Microbiology
- Vol. 5 (6) , 1331-1336
- https://doi.org/10.1111/j.1365-2958.1991.tb00779.x
Abstract
The arsR gene encodes the regulatory protein of the plasmid-encoded arsenical resistance operon. A series of in-frame fusions was constructed between the C-terminally truncated arsR gene and the coding region for the mature form of β-lactamase (blaM). Fusions containing most of the arsR gene were still inducible by arsenicals. Fusions containing less than 102 residues of the 117-residue ArsR protein were constitutive. When a wild-type arsR gene was placed in trans, the constitutive constructs were again inducible. The results demonstrate that the ArsR protein is a trans-acting regulatory protein which controls its own expression.Keywords
This publication has 17 references indexed in Scilit:
- Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetiiCellular Microbiology, 2007
- β‐lactamase as a probe of membrane protein assembly and protein exportMolecular Microbiology, 1990
- Molecular analysis of an ATP-dependent anion pumpPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1990
- Cadmium resistance from Staphylococcus aureus plasmid pI258 cadA gene results from a cadmium-efflux ATPase.Proceedings of the National Academy of Sciences, 1989
- A vector for the construction of translational fusions to TEM β-lactamase and the analysis of protein export signals and membrane protein topologyGene, 1986
- A plasmid-encoded arsenite pump produces arsenite resistance in Escherichia coliBiochemical and Biophysical Research Communications, 1984
- Cloning and expression of R-factor mediated arsenate resistance in Escherichia coliMolecular Genetics and Genomics, 1983
- Energetics of plasmid-mediated arsenate resistance in Escherichia coli.Proceedings of the National Academy of Sciences, 1982
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences, 1977
- Novel Method for Detection of β-Lactamases by Using a Chromogenic Cephalosporin SubstrateAntimicrobial Agents and Chemotherapy, 1972