z-logo
open-access-imgOpen Access
Reduced cadmium transport determined by a resistance plasmid in Staphylococcus aureus
Author(s) -
Z Tynecka,
Z Goś,
J.M. Zajac
Publication year - 1981
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.147.2.305-312.1981
Subject(s) - efflux , strain (injury) , staphylococcus aureus , plasmid , cadmium , antiporter , biology , microbiology and biotechnology , transporter , kinetics , escherichia coli , biophysics , biochemistry , bacteria , nuclear chemistry , chemistry , gene , genetics , physics , organic chemistry , quantum mechanics , membrane , anatomy
The presence of a plasmid harboring a gene for Cd2+ resistance led to markedly reduced Cd2+ uptake via the energy-dependent Mn2+ transport system in Staphylococcus aureus strain 17810R. Cd2+ uptake by the resistant strain via this high-affinity system was seen only at very low Cd2+ concentrations. At high concentrations, Cd2+ was taken up by the resistant strain via a different low-affinity uptake system. Cd2+ uptake via this system was energy dependent but was not blocked by Mn2+. Loss of the plasmid from the resistant strain resulted in Cd2+ sensitivity and unblocking of Cd2+ transport via the Mn2+ carrier in the plasmidless derivative strain 17810S. The energy-dependent Cd2+ uptake by the sensitive strain was inhibited by Mn2+ with kinetics indicating competitive inhibition. It is suggested that the second, low-affinity uptake system for Cd2+ in the resistant strain is the energy-dependent cadmium/proton antiporter, which at low Cd2+ concentrations functions in net Cd2+ efflux.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom