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J Bacteriol. Aug 1995; 177(15): 4207–4215.
PMCID: PMC177164

Identification of cutC and cutF (nlpE) genes involved in copper tolerance in Escherichia coli.

Abstract

It has been suggested previously that copper transport in Escherichia coli is mediated by the products of at least six genes, cutA, cutB, cutC, cutD, cutE, and cutF. A mutation in one or more of these genes results in an increased copper sensitivity (D. Rouch, J. Camakaris, and B. T. O. Lee, p. 469-477, in D. H. Hamer and D. R. Winge, ed., Metal Ion Homeostasis: Molecular Biology and Chemistry, 1989). Copper-sensitive cutC and cutF mutants were transformed with a genomic library of E. coli, and copper-tolerant transformants were selected. Two distinct clones were identified, each of which partially restores copper tolerance in both the cutC and cutF mutants of E. coli. Subcloning, physical mapping, and sequence analysis have revealed that the cutC gene is located at 42.15 min on the E. coli genome and encodes a cytoplasmic protein of 146 amino acids and that the cutF gene is located at 4.77 min on the E. coli genome and is allelic to the nlpE gene independently identified by Silhavy and coworkers (W. B. Snyder, L. J. B. Davis, P. N. Danese, C. L. Cosma, and T. J. Silhavy, J. Bacteriol. 177:4216-4223, 1995). Results from the genetic mapping of the copper-sensitive mutations in the cutF mutant and sequencing of the cutC and cutF (nlpE) alleles from both cutC and cutF mutants indicate that both the cutC and cutF mutants are in fact double mutants altered in these two genes, and mutations in both the genes appear to be required for the copper-sensitive phenotype in each mutant.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Alex LA, Reeve JN, Orme-Johnson WH, Walsh CT. Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum delta H. Biochemistry. 1990 Aug 7;29(31):7237–7244. [PubMed]
  • Brown NL, Rouch DA, Lee BT. Copper resistance determinants in bacteria. Plasmid. 1992 Jan;27(1):41–51. [PubMed]
  • Bull PC, Cox DW. Wilson disease and Menkes disease: new handles on heavy-metal transport. Trends Genet. 1994 Jul;10(7):246–252. [PubMed]
  • Cha JS, Cooksey DA. Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins. Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):8915–8919. [PMC free article] [PubMed]
  • Craigen WJ, Cook RG, Tate WP, Caskey CT. Bacterial peptide chain release factors: conserved primary structure and possible frameshift regulation of release factor 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3616–3620. [PMC free article] [PubMed]
  • Crooke H, Cole J. The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain. Mol Microbiol. 1995 Mar;15(6):1139–1150. [PubMed]
  • Dancis A, Haile D, Yuan DS, Klausner RD. The Saccharomyces cerevisiae copper transport protein (Ctr1p). Biochemical characterization, regulation by copper, and physiologic role in copper uptake. J Biol Chem. 1994 Oct 14;269(41):25660–25667. [PubMed]
  • Dancis A, Yuan DS, Haile D, Askwith C, Eide D, Moehle C, Kaplan J, Klausner RD. Molecular characterization of a copper transport protein in S. cerevisiae: an unexpected role for copper in iron transport. Cell. 1994 Jan 28;76(2):393–402. [PubMed]
  • Danese PN, Snyder WB, Cosma CL, Davis LJ, Silhavy TJ. The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP. Genes Dev. 1995 Feb 15;9(4):387–398. [PubMed]
  • Elliott T. Cloning, genetic characterization, and nucleotide sequence of the hemA-prfA operon of Salmonella typhimurium. J Bacteriol. 1989 Jul;171(7):3948–3960. [PMC free article] [PubMed]
  • Eriani G, Delarue M, Poch O, Gangloff J, Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature. 1990 Sep 13;347(6289):203–206. [PubMed]
  • Eriani G, Dirheimer G, Gangloff J. Isolation and characterization of the gene coding for Escherichia coli arginyl-tRNA synthetase. Nucleic Acids Res. 1989 Jul 25;17(14):5725–5736. [PMC free article] [PubMed]
  • Fong ST, Camakaris J, Lee BT. Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12. Mol Microbiol. 1995 Mar;15(6):1127–1137. [PubMed]
  • Gupta SD, Gan K, Schmid MB, Wu HC. Characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in apolipoprotein N-acyltransferase. J Biol Chem. 1993 Aug 5;268(22):16551–16556. [PubMed]
  • Jobling MG, Holmes RK. Construction of vectors with the p15a replicon, kanamycin resistance, inducible lacZ alpha and pUC18 or pUC19 multiple cloning sites. Nucleic Acids Res. 1990 Sep 11;18(17):5315–5316. [PMC free article] [PubMed]
  • Kadner RJ, Heller K, Coulton JW, Braun V. Genetic control of hydroxamate-mediated iron uptake in Escherichia coli. J Bacteriol. 1980 Jul;143(1):256–264. [PMC free article] [PubMed]
  • Kohara Y, Akiyama K, Isono K. The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell. 1987 Jul 31;50(3):495–508. [PubMed]
  • Mattar S, Scharf B, Kent SB, Rodewald K, Oesterhelt D, Engelhard M. The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation. J Biol Chem. 1994 May 27;269(21):14939–14945. [PubMed]
  • Mellano MA, Cooksey DA. Nucleotide sequence and organization of copper resistance genes from Pseudomonas syringae pv. tomato. J Bacteriol. 1988 Jun;170(6):2879–2883. [PMC free article] [PubMed]
  • Odermatt A, Suter H, Krapf R, Solioz M. Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J Biol Chem. 1993 Jun 15;268(17):12775–12779. [PubMed]
  • Parales RE, Harwood CS. Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida. J Bacteriol. 1992 Jul;174(14):4657–4666. [PMC free article] [PubMed]
  • Pel HJ, Maat C, Rep M, Grivell LA. The yeast nuclear gene MRF1 encodes a mitochondrial peptide chain release factor and cures several mitochondrial RNA splicing defects. Nucleic Acids Res. 1992 Dec 11;20(23):6339–6346. [PMC free article] [PubMed]
  • Pel HJ, Rep M, Grivell LA. Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure. Nucleic Acids Res. 1992 Sep 11;20(17):4423–4428. [PMC free article] [PubMed]
  • Ritonja A, Krizaj I, Mesko P, Kopitar M, Lucovnik P, Strukelj B, Pungercar J, Buttle DJ, Barrett AJ, Turk V. The amino acid sequence of a novel inhibitor of cathepsin D from potato. FEBS Lett. 1990 Jul 2;267(1):13–15. [PubMed]
  • Rogers SD, Bhave MR, Mercer JF, Camakaris J, Lee BT. Cloning and characterization of cutE, a gene involved in copper transport in Escherichia coli. J Bacteriol. 1991 Nov;173(21):6742–6748. [PMC free article] [PubMed]
  • Singer M, Baker TA, Schnitzler G, Deischel SM, Goel M, Dove W, Jaacks KJ, Grossman AD, Erickson JW, Gross CA. A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli. Microbiol Rev. 1989 Mar;53(1):1–24. [PMC free article] [PubMed]
  • Snyder WB, Davis LJ, Danese PN, Cosma CL, Silhavy TJ. Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway. J Bacteriol. 1995 Aug;177(15):4216–4223. [PMC free article] [PubMed]
  • Snyder WB, Silhavy TJ. Beta-galactosidase is inactivated by intermolecular disulfide bonds and is toxic when secreted to the periplasm of Escherichia coli. J Bacteriol. 1995 Feb;177(4):953–963. [PMC free article] [PubMed]
  • Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J Mol Biol. 1990 Oct 5;215(3):403–410. [PubMed]
  • Tetaz TJ, Luke RK. Plasmid-controlled resistance to copper in Escherichia coli. J Bacteriol. 1983 Jun;154(3):1263–1268. [PMC free article] [PubMed]
  • Zhou Z, Syvanen M. Identification and sequence of the drpA gene from Escherichia coli. J Bacteriol. 1990 Jan;172(1):281–286. [PMC free article] [PubMed]

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