A new class of proteins capable of binding transition metals

Plant Molecular Biology

Volumn 41, Issue 1, 1999, Pages 139-150

  Dykema, Philip E ^a   Sipes, Philip R ^a   Marie, Anne ^a   Biermann, Brenda J ^a   Crowell, Dring N ^a   Randall, Stephen K ^a  

^a INDIANA UNIVERSITY   (United States)

Author keywords

Arabidopsis thaliana; Isoprenylated protein; Metal binding protein

Indexed keywords

PLANT DEVELOPMENT; PLANT GROWTH; PROTEIN ANALYSIS; PROTEIN BINDING;

AMINO ACID SEQUENCE; ARABIDOPSIS; BINDING SITES; CHROMATOGRAPHY, AFFINITY; DNA, COMPLEMENTARY; EXONS; GENES, PLANT; INTRONS; METALS; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PLANTS, TOXIC; PROTEIN BINDING; PROTEIN ISOPRENYLATION; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; TOBACCO;

ARABIDOPSIS; ARABIDOPSIS THALIANA; ESCHERICHIA COLI; GLYCINE MAX; NICOTIANA TABACUM;

EID: 0033197670     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006367609556     Document Type: Article

References (57)

1. Altschul, S.F., Gish, W., Miller, W., Myers, E.W. and Lipman, D.J. 1990. Basic local alignment search tool. J. Mol. Biol. 215: 403-410.
2. Anant J.S., Ong, O.C., Xie, H., Clarke, S., O'Brien, P.J. and Fung, B.K.-K. 1992. In vivo differential prenylation of retinal cyclic GMP phosphodiesterase catalytic subunits. J. Biol. Chem. 267: 687-690.
3. Biermann, B.J., Morehead, T.A., Tate, S.E., Price, J.R., Randall, S.K. and Crowell, D.N. 1994. Novel isoprenylated proteins identified by an expression library screen. J. Biol. Chem. 269: 25251-25254.
4. Brown, J.C. and Jones, W.E. 1974. pH changes associated with iron-stress response. Physiol. Plant. 30: 148-152.
5. Brown, N.L., Camakaris, J., Lee, B.T.O., Williams, T., Morby, A.P., Parkhil, J. and Rouch, D.A. 1991. Bacterial resistances to mercury and copper. J. Cell Biochem. 46: 106-114.
6. Buckhout, T.J., Bell, P.F., Luster, D.G. and Chaney, R.L. 1989. Iron-stress induced redox activity in tomato (Lycopersicon esculentum Mill.) is localized on the plasma membrane. Plant Physiol. 90: 151-156.
7. Bull, P.C., Thomas, G.R., Rommens, J.M., Forbes, J.R. and Cox, D.W. 1993. The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene. Nature Genet. 5: 327-337.
8. Caplin, B.E. and Marshall, M.S. 1995. Mutagenesis and biochemical analysis of recombinant yeast prenyltransferases. Meth. Enzymol. 250: 51-68.
9. CAAX protein tyrosine phosphatases. Cancer Lett. 110: 49-55.
10. Chaney, R.L. 1987. Complexity of iron nutrition: lessons for plant-soil interaction research. J. Plant Nutr. 10: 963-994.
11. Chavrier, P., Parton, R.G., Hauri, H.P., Simons, K. and Zerial, M. 1990. Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell 62: 317-329.
12. Clapham, D.E. and Neer, E.J. 1993. New roles for G-protein βγ-dimers in transmembrane signalling. Nature 365: 403-406.
13. Clarke, S. 1992. Protein isoprenylation and methylation at carboxylterminal cysteine residues. Annu. Rev. Biochem. 61: 355-386.
14. Crowell, D.N. and Amasino, R.M. 1991. Induction of specific mRNAs in cultured soybean cells during cytokinin or auxin starvation. Plant Physiol. 95: 711-715.
15. Crowell, D.N., Biermann, B.J. and Randall, S.K. 1996. Identification of cDNAs encoding isoprenylated proteins. Mol. Biotechnol. 5: 253-258.
16. Culotta, V.C., Klomp, L.W.J., Strain, J., Casareno, R.H.B., Krems, B. and Gitlin, J.D. 1997. The copper chaperone for superoxide dismutase. J. Biol. Chem. 272: 23469-23472.
17. D'Alessio, J.M., Bebee, R., Hartley, J.L., Noon, M.C. and Polayes, D. 1992. Lambda ZipLox: automatic subcloning of cDNA. Focus 14: 76 (1992).
18. Dancis, A., Yuan, D.S., Haile, D., Aswith, C., Eide, D., Moehle, C., Kaplan, J. and Klausner, R.D. 1994. Molecular characterization of a copper transporter protein in S. cerevisiae: an unexpected role for copper in iron transport. Cell 76: 393-402.
19. Eide, D., Broderius, M., Fett, J. and Guerinot, M.L. 1996. A novel iron-regulated metal transporter from plants identified by functional expression in yeast. Proc. Natl. Acad. Sci. USA, 93: 5624-5628.
20. Fox, T.C. and Guerinot, M.L. 1998. Molecular biology of cation transport in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49: 669-696.
21. Hancock, J.F., Cadwallader, K., Paterson, H. and Marshall, C.J. 1991. A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins. EMBO J. 10: 4033-4039.
22. Himelblau, E., Mira, H., Lin, S.-J., Culotta, V.C., Penarrubia, L. and Amasino, R.M. 1998. Identification of a functional homolog of the yeast copper homeostasis gene ATX1 from Arabidopsis. Plant Physiol. 117: 1227-1234.
23. Hung, I.H., Casareno, R.L.B., Labesse, G., Mathews, F.S. and Gitlin, J.D. 1998. HAH1 is a copper-binding protein with distinct amino acid residues mediating copper homeostasis and antioxidant defense. J. Biol. Chem. 273: 1749-1754.
24. Hwang, S.B. and Lai, M.M. 1993. Isoprenylation mediates direct protein-protein interactions between hepatitis large delta antigen and hepatitis B virus surface antigen. J. Virol. 67: 7659-7662.
25. Iida, M., Terada, K., Sambongi, Y., Wakabayashi, T., Miura, N., Koyama, K., Futai, M. and Sugiyama, T. 1998. Analysis of functional domains of Wilson disease protein (ATP7B) in Saccharomyces cerevisiae. FEBS Lett. 428: 281-285.
26. Inglese, J., Glickman, J.F., Lorenz, W., Caron, M.G. and Lefkowitz, R.J. 1992. Isoprenylation of a protein kinase: requirement of farnesylation/α-carboxyl methylation for full enzymatic activity of rhodopsin kinase. J. Biol. Chem. 267: 1422-1425.
27. Jiang, W., Graham, B., Spiccia, L. and Hearn, M.T.W. 1998. Protein selectivity with immobilized metal ion-tacn sorbents: chromatographic studies with human serum proteins and several other globular proteins. Anal. Biochem. 255: 47-58.
28. Johnson, R.D., Todd, R.J. and Arnold, F.H. 1996. Multipoint binding in metal-affinity chromatography II. Effect of pH and imidazole on chromatographic retention of engineered histidine-containing cytochromes c. J. Chromat. A 725: 225-235.
29. Kuchler, K., Sterne, R.E. and Thorner, J. 1989. Saccharomyces cerevisiae STE6 gene product: a novel pathway for protein export in eukaryotic cells. EMBO J. 8: 3973-3984.
30. Lin, S.-J. and Culotta, V.C. 1995. The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity. Proc. Natl. Acad. Sci. USA 92: 3784-3788.
31. Lin, S.-J., Pufahl, R.A., Dancis, A., O'Halloran, T.V. and Culotta, V.C. 1997. A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport. J. Biol. Chem. 272: 9215-9220.
32. Lowy, D.R. and Willumsen, B.M. 1993. Function and regulation of Ras. Annu. Rev. Biochem. 62: 851-891.
33. Lutsenko, S., Petrukin, K., Cooper, M.J., Gilliam, C.T. and Kaplan, J.H. 1997. N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat. J. Biol. Chem. 272: 18939-18944.
34. Marcus, S., Caldwell, G.A., Miller, D., Xue, C.-B., Naider, F. and Becker, J.M. 1991. Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiae a-factor mating pheromone. Mol. Cell. Biol. 11: 3606-3612.
35. Marjorette, M., Pena, O., Koch, K.A. and Thiele, D.J. 1998. Dynamic regulation of copper uptake and detoxification genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 18: 2514-2523.
36. Muller, K.M., Arndt, K.M., Bauer, K. and Pluckthun, A. 1998. Tandem immobilized metal-ion affinity chromatography/immunoaffinity purification of His-tagged proteins: evaluation of two anti-His tag monoclonal antibodies. Anal. Biochem. 259: 54-61.
37. Nakamura, Y., Sato, S., Kanato, T., Kotani, H., Asamizu, E., Miyajima, N. and Tataba, S. 1997. Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions 1,191,918 bp covered by seventeen physically assigned P1 clones. DNA Res. 4: 410-414.
38. Newman, T., de Bruijn, F.J., Green, P., Keegstra, K., Kende, H., McIntosh, L., Ohlrogge, J., Raikel, N., Somerville, S., Thomashow, M., Retzel, E. and Somerville, C. 1994. Genes galore: a summary of methods for accessing results from large-scale partial sequencing of anonymous Arabiopsis cDNA clones. Plant Physiol. 106: 1241-1255.
39. Ouariti, O., Boussama, N., Zarrouk, M., Cherif, A. and Ghorbal, M.H. 1997. Cadmium- and copper-induced changes in tomato membrane lipids. Phytochemistry 45: 1343-1350.
40. Payne, A.S. and Gitlin, J.D. 1998. Functional expression of the Menkes disease protein reveals common biochemical mechanisms among the copper-transporting P-type ATPases. J. Biol. Chem. 273: 3765-3770.
41. Predki, P.F. and Sarkar, B. 1992. Effect of replacement of 'zinc finger' zinc on estrogen receptor DNA interactions J. Biol. Chem. 267: 5842-5846.
42. Randall, S.K. and Crowell, D.N. 1997. Protein isoprenylation in plants. In: E.J. Parish and W.D. Nes (Eds.), Biochemistry and Function of Sterols, CRC Press, New York, pp. 231-244.
43. Randall, S.K., Marshall, M.S. and Crowell, D.N. 1993. Protein isoprenylation in suspension-cultured tobacco cells. Plant Cell 5: 433-442.
44. Rauser, W.E. 1990. Phytochelatins. Annu. Rev. Biochem. 59: 61-86.
45. Rief, O.-W., Nier, V., Bahr, U. and Freitag, R. 1994. Immobilized metal affinity membrane adsorbers as stationary phases for metal interaction protein separation. J. Chromat. A664: 13-25.
46. Robinson, N.J., Tommey, A.M., Kuske, C. and Jackson, P.J. 1993. Plant metallothioneins. Biochem. J. 295: 1-10.
47. Sahlman, L. and Skarfsted, E.G. 1993. Mercuric ion binding abilities of MerP variants containing only one cysteine. Biochem. Biophys. Res. Comm. 196: 583-588.
48. Sambrook, J., Fritsch, E.F. and Maniatis, T. 1989. Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Press, Cold Spring Harbor, NY.
49. Stohs, S.J. and Bagchi, D. 1995. Oxidative mechanisms in the toxicity of metal ions. Free Rad. Biol. Med. 18: 321-336.
50. Tanaka, T., Ames, J.B., Harvey, T.S., Stryer, L. and Ikura, M. 1995. Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature 376: 444-447.
51. Venkat Raju, K. and Marschner, H. 1972. Regulation of iron uptake from relatively insoluble iron compounds by sunflower plants. Z. Pflanzenernaehr. Bodenkd. 132: 177-190.
52. Volz, J., Bosch, F.U., Wunderlin, M., Schuhmacher, M., Melchers, K., Bensch, K., Steinhilber, W., Schafer, K.P., Toth, G., Penke, B. and Przybylski, M. 1998. Molecular characterization of metal-binding polypeptide domains by electrospray ionization mass spectrometry and metal chelate affinity chromatography. J. Chromat. A 800: 29-37.
53. Vorburger, K., Kitten, G.T. and Nigg, E.A. 1989. Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lystates and requires the cysteine residue of the C-terminal CXXM motif. EMBO J. 8: 4007-4013.
54. Vulpe, C.D. and Packman, S. 1995. Cellular copper transport. Annu. Rev. Nutr. 15: 293-322.
55. Zachariou, M. and Hearn, M.T.W. 1996. Application of immobilized metal ion chelate complexes as pseudocation exchange absorbents for protein separation. Biochemistry 35: 202-211.
56. Zhang, F.L. and Casey, P.J. 1996. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65: 241-269.
57. Zhu, J.-K., Bressan, R.A. and Hasegawa, P.M. 1993. Isoprenylation of the plant molecular chaperone ANJ1 facilitates membrane association and function at high temperature. Proc. Natl. Acad. Sci. USA 90: 8557-8561.