regulation of the staphylococcus aureus plasmid pi258 mercury resistance operon.experiments involving fusion between the staphylococcus aureus plasmid pi258-encoded mer operon and the reporter gene beta-lactamase, mutational analysis, and trans-complementation studies have shown that the merr gene of pi258, which shows dna sequence similarity with known merr genes from other bacteria, regulates the expression of the mer operon in vivo. the merr gene product is a trans-acting protein that activates mer operon transcription in the presence of the inducers hg2+ and cd2+. a glu ...19921400255
luxab gene fusions with the arsenic and cadmium resistance operons of staphylococcus aureus plasmid pi258.pc101, a novel shuttle vector between escherichia coli and staphylococcus aureus carrying the lux genes encoding luciferase from vibrio harveyi, selectable ampicillin and chloramphenicol markers and origins of replication for gram-negative and gram-positive bacteria has been constructed. the inducibility of the arsenic and cadmium operon from s. aureus plasmid pi258 to different ions has been tested in e. coli and in s. aureus with two fusions in pc101: an arsb-luxab and a cada-luxab transcripti ...19938349095
pb(ii)-translocating p-type atpases.the cad operon of staphylococcus aureus plasmid pi258, which confers cadmium resistance, encodes a transcriptional regulator, cadc, and cada, an atp-coupled cd(ii) pump that is a member of the superfamily of cation-translocating p-type atpases. the escherichia coli homologue of cada, termed znta, is a zn(ii)/cd(ii) pump. the results described in this paper support the hypothesis that znta and cada are pb(ii) pumps. first, cadc is a metal-responsive repressor that responds to soft metals in the o ...19989830000
specific potassium binding stabilizes pi258 arsenate reductase from staphylococcus aureus.arsenate reductase (arsc) from staphylococcus aureus plasmid pi258 catalyzes the reduction of arsenate to arsenite and plays a role in bacterial heavy metal resistance. the high resolution x-ray structure of arsc reveals the atomic details of the k+ binding site situated next to the catalytic p-loop structural motif of this redox enzyme. a full thermodynamic study of the binding characteristics of a series of monovalent cations (li+, na+, k+, rb+, and cs+) and their influence on the thermal stab ...200312682056
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