Abstract
Mercury resistance shown by a strain of Enterobacter aerogenes was found to be determined by a plasmid. The resistance appeared to be not due to enzymatic volatilization of mercury, but due to the alteration in cellular permeability to mercury.
Comparison of the outer membrane proteins was made between the resistant cells and the sensitive counterparts obtained by the treatment with mitomycin C, showing that two proteins with molecular weight of 46,000 and 44,000 had disappeared from the outer membrane along with the plasmid by the curing. These results suggest that the two membrane proteins mediating the cellular permeability to mercury compound may be responsible for the mercury resistance of the strain.
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References
Chopra I (1971) Decreased uptake of cadmium by a resistant strain of Staphylococcus aureus. J Gen Microbiol 63:265–267
Clark DK, Weiss AA, Silver S (1977) Mercury and organomercurial resistance determined by plasmid in Pseudomonas. J Bacteriol 132:186–196
Greenaway W (1972) Permeability of phenyl-Hg+-resistant and phenyl-Hg+-susceptible isolates of Pyrenophore avenae to the phenyl-Hg+ ion. J Gen Microbiol 73:251–255
Hansen JB, Olsen RH (1978) Isolation of large bacterial plasmids and characterization of the P2 incompatibility group plasmids PMG1 and PMG5. J Bacteriol 135:227–238
Horitsu H, Ito T (1980) Comparisons of characteristics of mercury tolerant bacterium Pseudomonas oleovorans G-1 and its mercury sensitive mutant strain. Agric Biol Chem 44:2317–2322
Ishihara M, Kamio Y, Terawaki Y (1978) Cupric ion resistance as a new genetic marker of a temperature sensitive R plasmid, Rtsl in Escherichia coli. Biochem Biophys Res Commun 82:74–80
Komura I, Izaki K (1971) Mechanism of mercuric chloride resistance in microorganisms. 1. Vaporization of a mercury compound from mercuric chloride by multiple drug resistance strain of Escherichia coli. J Biochem 70:885–893
Kondo I, Ishikawa T, Nakahara H (1974) Mercury and cadmium resistance mediated by the penicillinase plasmid in Staphylococcus aureus. J Bacteriol 117:1–7
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
Lutkenhaus JF (1977) Role of a major outer membrane protein in Escherichia coli. J Bacteriol 131:631–637
Manning PA, Beutin L, Achtman M (1980) Outer membrane of Escherichia coli. Properties of the F sex factor tra T protein which is involved in surface exclusion. J Bacteriol 142:285–294
Miura T, Mizushima S (1969) Separation and properties of outer and cytoplasmic membranes in Escherichia coli. Biochim Biophys Acta 193:268–276
Pan-Hou HSK, Imura N (1981) Role of hydrogen sulfide in mercury resistance determined by plasmid of Clostridium cochlearium T-2. Arch Microbiol 129:49–52
Schnaitman CA (1971) Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100. J Bacteriol 108:545–552
Schottel J, Mandal A, Clark D, Silver S (1974) Volatilization of mercury and organomercurials determined by inducible R-factor in enteric bacteria. Nature 251:335–337
Schottel JL (1978) The mercuric and organomercurial detoxifying enzymes from a plasmid-bearing strain of Escherichia coli. J Biol Chem 253:4341–4349
Summers AO, Silver S (1972) Mercury resistance in a plasmid-bearing strain of Escherichia coli. 112:1228–1236
Summers AO, Silver S (1978) Microbial transformations of metals. Ann Rev Microbiol 32:637–672
Wang PY, Relf J, Palchaudhuri S, Iyer VN (1978) Plasmid coferring increased sensitivity to mercuric chloride and cobalt chloride found in some laboratory strain of Escherichia coli K-12. J Bacteriol 133:1042–1043
Weiss AA, Murphy SD, Silver S (1977) Mercury and organomercurial resistance determined by plasmid in Staphylococcus aureus. J Bacteriol 132:197–208
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Pan-Hou, H.S., Nishimoto, M. & Imura, N. Possible role of membrane proteins in mercury resistance of Enterobacter aerogenes . Arch. Microbiol. 130, 93–95 (1981). https://doi.org/10.1007/BF00411057
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DOI: https://doi.org/10.1007/BF00411057