CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA

FEMS Microbiology Letters

Volumn 220, Issue 1, 2003, Pages 105-112

  Radford, David S ^a   Kihlken, Margaret A ^b   Borrelly, Gilles P M ^a   Harwood, Colin R ^a   Le Brun, Nick E ^b   Cavet, Jennifer S ^a  

^a NEWCASTLE UNIVERSITY   (United Kingdom)

^b UNIVERSITY OF EAST ANGLIA   (United Kingdom)

Author keywords

Atx1; CopA; CopZ; Cytochrome oxidase; Metallochaperone; P type ATPase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CADMIUM; CHAPERONE; COPPER; CYTOCHROME C OXIDASE; PROTEIN COPZ; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BACILLUS SUBTILIS; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; TWO HYBRID SYSTEM;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS);

EID: 0347721765     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00095-8     Document Type: Article

References (48)

1. Fraústo da Silva, J.J.R. and Williams, R.J.P. (2001) The Biological Chemistry of the Elements: The Inorganic Chemistry of Life, 2nd edn. Clarenden Press, Oxford.
2. Rae T.D., Schmidt P.J., Pufahl R.A., Culotta V.C., O'Halloran T.V. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science. 284:1999;805-808.
3. Puig S., Thiele D.J. Molecular mechanisms of copper uptake and distribution. Curr. Opin. Chem. Biol. 6:2002;171-180.
4. O'Halloran T.V., Culotta V.C. Metallochaperones, an intracellular shuttle service for metal ions. J. Biol. Chem. 275:2000;25057-25060.
5. Harrison M.D., Jones C.E., Solioz M., Dameron C.T. Intracellular copper routing, the role of copper metallochaperones. Trends Biochem. Sci. 25:2000;29-32.
6. Tottey S., Rondet S.A.M., Borrelly G.P.M., Robinson P.J., Rich P.R., Robinson N.J. A copper metallochaperone for photosynthesis and respiration reveals metal-specific targets, interaction with an importer and alternative sites for copper acquisition. J. Biol. Chem. 277:2002;5490-5497.
7. Odermatt A., Solioz M. Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae. J. Biol. Chem. 270:1995;4339-4354.
8. Cobine P., Wickramasinghe W.A., Harrison M.D., Weberb T., Solioz M., Dameron C.T. The Enterococcus hirae copper chaperone CopZ delivers copper(I) to the CopY repressor. FEBS Lett. 445:1999;27-30.
9. 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. 268:1993;12775-12779.
10. Multhaup G., Strausak D., Bissig K.-D., Solioz M. Interaction of the CopZ copper chaperone with the CopA copper ATPase of Enterococcus hirae assessed by surface plasmon resonance. Biochem. Biophys. Res. Commun. 288:2001;172-177.
11. Banci L., Bertini I., Del Conte R., Markey J., Ruiz-Duenas F.J. Copper trafficking: the solution structure of Bacillus subtilis CopZ. Biochemistry. 40:2001;15660-15668.
12. Wimmer R., Herrmann T., Solioz M., Wuthrich K. NMR structure and metal interactions of the CopZ copper chaperone. J. Biol. Chem. 274:1999;22597-22603.
13. Rosenzweig A.C., Huffman D.L., Hou M.Y., Wernimont A.K., Pufahl R.A., O'Halloran T.V. Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution. Struct. Fold Des. 7:1995;605-617.
14. Arnesano F., Banci L., Bertini I., Huffman D.L., O'Halloran T.V. Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1. Biochemistry. 40:2001;1528-1539.
15. Banci L., Bertini I., Ciofi-Baffoni S., Huffman D.L., O'Halloran T.V. Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states. J. Biol. Chem. 276:2001;8415-8426.
16. Arnesano F., Banci L., Bertini I., Cantini F., Ciofi-Baffoni S., Huffman D.L., O'Halloran T.V. Characterization of the binding interface between the copper metallochaperone Atx1 and the first cytosolic domain of Ccc2 ATPase. J. Biol. Chem. 276:2001;41365-41376.
17. Banci L., Bertini I., Ciofi-Baffoni S., D'Onofrio M., Gonnelli L., Marhuenda-Egea C.F., Ruiz-Dueñas F.J. Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states. J. Mol. Biol. 317:2002;415-429.
18. Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., et al. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature. 390:1998;249-256.
19. Erlendsson L.S., Hederstedt L. Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells. J. Bacteriol. 84:2002;1423-1429.
20. Silver S., Phung L.T. Bacterial heavy metal resistance: new surprises. Annu. Rev. Microbiol. 50:1996;753-789.
21. Gatti D., Mitra B., Rosen B.P. Escherichia coli soft metal ion-translocating ATPases. J. Biol. Chem. 275:2000;34009-34012.
22. Nucifora G., Chu L., Misra T.K., Silver S. Cadmium resistance from Staphylococcus aureus plasmid pI258 cadA gene results from a cadmium-efflux ATPase. Proc. Natl. Acad. Sci. USA. 86:1989;3544-3548.
23. Beard S.J., Hashim R., Membrillo-Hernandez J., Hughes M.N., Poole R.K. Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase. Mol. Microbiol. 25:1997;883-891.
24. Rensing C., Mitra B., Rosen B.P. The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase. Proc. Natl. Acad. Sci. USA. 94:1997;14326-14331.
25. Thelwell C., Robinson N.J., Turner-Cavet J.S. An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc exporter. Proc. Natl. Acad. Sci. USA. 95:1998;10728-10733.
26. Rutherford J.C., Cavet J.S., Robinson N.J. Cobalt-dependent transcriptional switching by a dual-effector MerR-like protein regulates a cobalt-exporting variant CPx-type ATPase. J. Biol. Chem. 274:1999;25827-25832.
27. Gupta A., Matsui K., Lo J.F., Silver S. Molecular basis for resistance to silver cations in Salmonella. Nat. Med. 5:1999;183-188.
28. Rensing C., Fan B., Sharma R., Mitra B., Rosen B.P. CopA: An Escherichia coli Cu(I)-translocating P-type ATPase. Proc. Natl. Acad. Sci. USA. 97:2000;652-656.
29. Gaballa, A. and Helmann, J. (2002) Bacillus subtilis CPx-type ATPases: characterisation of Cd, Zn, Co and Cu efflux systems. Biometals, in press.
30. 2+ ion resistance. FEMS Microbiol. Lett. 208:2002;105-109.
31. Vagner V., Dervyn E., Ehrlich S.D. A vector for systematic gene inactivation in Bacillus subtilis. Microbiology. 144:1998;3097-3104.
32. Fortnagel P., Freese E. Analysis of sporulation mutants. II. Mutants blocked in the citric acid cycle. J. Bacteriol. 95:1968;1431-1438.
33. Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd edn. Cold Springs Harbor Laboratory, Cold Springs Harbor, NY.
34. Bron, S. (1990) Plasmids. In: Molecular Biological Methods for Bacillus (Harwood, C.R. and Cutting, S.M., Eds.), pp. 75-174. John Wiley and Sons Ltd., Chichester.
35. Guérout-Fleury A.-M., Shazand K., Frandsen N., Stragier P. Gene. 167:1995;335-336.
36. Morby A.P., Turner J.S., Huckle J.W., Robinson N.J. SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex. Nucleic Acids Res. 21:1993;921-925.
37. Le Brun N.E., Bengtsson J., Hederstedt L. Genes required for cytochrome c synthesis in Bacillus subtilis. Mol. Microbiol. 36:2000;638-650.
38. Hederstedt L. Molecular properties, genetics, and biosynthesis of Bacillus subtilis succinate dehydrogenase complex. Methods Enzymol. 126:1986;399-414.
39. 3-type oxidases. Mol. Microbiol. 5:1991;2063-2072.
40. Smith P.K., Krohn R.I., Hermanson G.T., Mallia A.K., Gartner F.H., Provenzano M.D., Fujimoto E.K., Goeke N.M., Olson B.J., Klenk D.C. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150:1985;76-85.
41. Paulsen I.T., Saier M.H. Jr. A novel family of ubiquitous heavy metal ion transport proteins. J. Membr. Biol. 156:1997;99-103.
42. Solioz M., Vulpe C. CPx-type ATPases: a class of P-type ATPases that pump heavy metals. Trends Biol. Sci. 21:1996;237-241.
43. Perkins J.B., Youngman J.C. Construction and properties of Tn917-lacZ, a transposon derivative that mediates transcriptional gene fusions in Bacillus subtilis. Proc. Natl. Acad. Sci. USA. 83:1986;140-144.
44. Kihlken M.A., Leech A.P., Le Brun N.E. Copper-mediated dimerisation of CopZ, a predicted copper chaperone from Bacillus subtilis. Biochem. J. 368:2002;729-739.
45. Tottey S., Rich P.R., Rondett S.A.M., Robinson N.J. Two Menkes-type ATPases supply copper for photosynthesis in Synechocystis PCC 6803. J. Biol. Chem. 276:2001;19999-20004.
46. Glerum D.M., Shtanko A., Tzagoloff A. SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J. Biol. Chem. 271:1996;20531-20535.
47. Nittis T., George G.N., Winge D.R. Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein. J. Biol. Chem. 276:2001;42520-42526.
48. Mattatall N.R., Jazaira J., Hill B.C. Characterization of YpmQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis. J. Biol. Chem. 275:2000;28802-28809.