Cu 2+ triggers reversible aggregation of a disordered His-rich dehydrin MpDhn12 from Musa paradisiaca

Journal of Biochemistry

Volumn 150, Issue 5, 2011, Pages 491-499

  Mu, Peiqiang ^a   Feng, Dongru ^a   Su, Jianbin ^a   Zhang, Yang ^a   Dai, Jinran ^a   Jin, Honglei ^a   Liu, Bing ^a   He, Yanming ^a   Qi, Kangbiao ^a   Wang, Hongbin ^a   Wang, Jinfa ^a  

^a SUN YAT SEN UNIVERSITY   (China)

Author keywords

aggregation; copper homoeostasis; Cu 2+ binding; dehydrin; disorder

Indexed keywords

COPPER ION; COPPER ZINC SUPEROXIDE DISMUTASE; DIETHYL PYROCARBONATE; ERD14 PROTEIN; HISTIDINE; MUSA PARADISIACA DEHYDRIN 12; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; COPPER; DEHYDRIN PROTEINS, PLANT;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARTICLE; BANANA; BINDING AFFINITY; CHELATION; CIRCULAR DICHROISM; CONTROLLED STUDY; IMMOBILIZED METAL AFFINITY CHROMATOGRAPHY; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR CLONING; MOLECULAR WEIGHT; MUSA PARADISIACA; NONHUMAN; NUCLEOTIDE SEQUENCE; PHENOTYPE; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; THERMOSTABILITY; YEAST; AFFINITY CHROMATOGRAPHY; CHEMISTRY; DRUG EFFECT; GENETIC COMPLEMENTATION; METABOLISM; MOLECULAR GENETICS; MUSA; SEQUENCE ALIGNMENT;

MUSA X PARADISIACA;

AMINO ACID SEQUENCE; BASE SEQUENCE; CHROMATOGRAPHY, AFFINITY; CIRCULAR DICHROISM; COPPER; GENETIC COMPLEMENTATION TEST; MOLECULAR SEQUENCE DATA; MUSA; PLANT PROTEINS; PROTEIN BINDING; SEQUENCE ALIGNMENT;

EID: 80155201810     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvr082     Document Type: Article

References (51)

1. O'Dell, B.L. (1976) Biochemistry of copper. Med. Clin. North Am. 60, 687-703
2. Burkhead, J.L., Reynolds, K.A., Abdel-Ghany, S.E., Cohu, C.M., and Pilon, M. (2009) Copper homeostasis. New Phytol. 182, 799-816
3. Mittler, R., Vanderauwera, S., Gollery, M., and Van Breusegem, F. (2004) Reactive oxygen gene network of plants. Trends Plant Sci. 9, 490-498
4. Yu, Z.L., Zhang, J.G., Wang, X.C., and Chen, J. (2008) Excessive copper induces the production of reactive oxygen species, which is mediated by phospholipase D, nicotinamide adenine dinucleotide phosphate oxidase and antioxidant systems. J. Integr. Plant Biol. 50, 157-167
5. Dastych, M. (1997) Copper-biochemistry, metabolism and physiologic function. Cas Lek Cesk. 136, 670-673
6. Palmer, C.M. and Guerinot, M.L. (2009) Facing the challenges of Cu, Fe and Zn homeostasis in plants. Nat. Chem. Biol. 5, 333-340
7. Puig, S. and Thiele, D.J. (2002) Molecular mechanisms of copper uptake and distribution. Curr. Opin. Chem. Biol. 6, 171-180
8. Rauser, W. (1999) Structure and function of metal chelators produced by plants. Cell Biochem. Biophys. 31, 19-48
9. Clemens, S. (2001) Molecular mechanisms of plant metal tolerance and homeostasis. Planta 212, 475-486
10. Vazquez, S., Goldsbrough, P., and Carpena, R.O. (2009) Comparative analysis of the contribution of phytochelatins to cadmium and arsenic tolerance in soybean and white lupin. Plant Physiol. Biochem. 47, 63-67
11. Guo, W.J., Meetam, M., and Goldsbrough, P.B. (2008) Examining the specific contributions of individual Arabidopsis metallothioneins to copper distribution and metal tolerance. Plant Physiol. 146, 1697-1706
12. Cobbett, C. and Goldsbrough, P. (2002) Phytochelatins and metallothioneins: Roles in heavy metal detoxification and homeostasis. Annu. Rev. Plant Biol. 53, 159-182
13. Zhou, J. and Goldsbrough, P.B. (1994) Functional homologs of fungal metallothionein genes from Arabidopsis. Plant Cell 6, 875-884
14. Vasak, M. (2005) Advances in metallothionein structure and functions. J. Trace Elem. Med. Biol. 19, 13-17
15. Rauser, W.E. (1995) Phytochelatins and related peptides. Structure, biosynthesis, and function. Plant Physiol. 109, 1141-1149
16. Cobbett, C.S. (2000) Phytochelatin biosynthesis and function in heavy-metal detoxification. Curr. Opin. Plant Biol. 3, 211-216
17. Pal, R. and Rai, J.P. (2010) Phytochelatins: Peptides involved in heavy metal detoxification. Appl. Biochem. Biotechnol. 160, 945-963
18. Andreini, C., Bertini, I., and Rosato, A. (2004) A hint to search for metalloproteins in gene banks. Bioinformatics 20, 1373-1380
19. DeSilva, T.M., Veglia, G., Porcelli, F., Prantner, A.M., and Opella, S.J. (2002) Selectivity in heavy metal- binding to peptides and proteins. Biopolymers 64, 189-197
20. Kung, C.C., Huang, W.N., Huang, Y.C., and Yeh, K.C. (2006) Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry. Proteomics 6, 2746-2758
21. Rorat, T. (2006) Plant dehydrins-tissue location, structure and function. Cell Mol. Biol. Lett. 11, 536-556
22. Close, T.J. (1997) Dehydrins: A commonalty in the response of plants to dehydration and low temperatureed. Physiol. Plant. 100, 291-296
23. Hara, M. (2010) The multifunctionality of dehydrins: An overview. Plant Signal. Behavior 5, 503-508
24. Close, T.J. (1996) Dehydrins: Emergence of a biochemical role of a family of plant dehydration proteinsed. Physiol. Plant. 97, 795-803
25. Kruger, C., Berkowitz, O., Stephan, U.W., and Hell, R. (2002) A metal-binding member of the late embryogenesis abundant protein family transports iron in the phloem of Ricinus communis L. J. Biol. Chem. 277, 25062-25069
26. Hara, M., Fujinaga, M., and Kuboi, T. (2005) Metal binding by citrus dehydrin with histidine-rich domains. J. Exp. Bot. 56, 2695-2703
27. Svensson, J., Palva, E.T., and Welin, B. (2000) Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography. Protein Expres. Purif. 20, 169-178
28. Jain, S.M., Priyadarshan, P.M., Bakry, F., Carreel, F., Jenny, C., and Horry, J.-P. (2009) Genetic improvement of banana. Breeding Plantation Tree Crops: Tropical Species, pp. 3-50, Springer, New York
29. Dai, J.R., Liu, B., Feng, D.R., Liu, H.Y., He, Y.M., Qi, K.B., Wang, H.B., and Wang, J.F. (2011) MpAsr encodes an intrinsically unstructured protein and enhances osmotic tolerance in transgenic Arabidopsis. Plant Cell Rep. 30, 1219-1230
30. Feng, D.R., Liu, B., Li, W.Y., He, Y.M., Qi, K.B., Wang, H.B., and Wang, J.F. (2009) Over-expression of a cold-induced plasma membrane protein gene (MpRCI) from plantain enhances low temperatureresistance in transgenic tobacco. Environ. Exp. Bot. 65, 395-402
31. Jin, X.L., Feng, D.R., Wang, H.B., and Wang, J.F. (2007) A novel tissue-specific plantain b-1,3-glucanase gene that is regulated in response to infection by Fusarium oxysporum fsp. cubense. Biotechnol. Lett. 29, 1431-1437
32. Fan, J.M., Wang, H.B., Feng, D.R., Liu, B., Liu, H.R., and Wang, J.F. (2007) Molecular Characterization of Plantain Class I Chitinase Gene and its Expression in Response to Infection by Gloeosporium musarum Cke and Massee and other Abiotic Stimuli. J. Biochem. 142, 561-570
33. Hu, Y.X., Guo, J.Y., Shen, L., Chen, Y., Zhang, Z.C., and Zhang, Y.L. (2002) Get effective polyclonal antisera in one month. Cell Res. 12, 157-160
34. Crowther, J.R. (1998) Enzyme-Linked Immunosorbent Assay (ELISA) Molecular Biomethods Handbook (Rapley, R. and Walker, J.M., eds.), pp. 595-617, Humana Press Inc, Totowa, NJ
35. Miles, E.W. (1977) Modification of histidyl residues in proteins by diethylpyrocarbonate. Methods Enzymol. 47, 431-442
36. Ueda, E.K., Gout, P.W., and Morganti, L. (2003) Current and prospective applications of metal ion-protein binding. J. Chromatogr. A 988, 1-23
37. Nishikawa, T., Lee, I.S., Shiraishi, N., Ishikawa, T., Ohta, Y., and Nishikimi, M. (1997) Identification of S100b protein as copper-binding protein and its suppression of copper-induced cell damage. J. Biol. Chem. 272, 23037-23041
38. Gietz, R.D., Schiestl, R.H., Willems, A.R., and Woods, R.A. (1995) Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11, 355-360
39. Smith, S.D., She, Y.M., Roberts, E.A., and Sarkar, B. (2004) Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J. Proteome Res. 3, 834-840
40. Receveur-Brechot, V., Bourhis, J.M., Uversky, V.N., Canard, B., and Longhi, S. (2006) Assessing protein disorder and induced folding. Proteins 62, 24-45
41. Tompa, P. (2002) Intrinsically unstructured proteins. Trends Biochem. Sci. 27, 527-533
42. Kovacs, D., Kalmar, E., Torok, Z., and Tompa, P. (2008) Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiol. 147, 381-390
43. Tanaka, Y., Tsumoto, K., Nakanishi, T., Yasutake, Y., Sakai, N., Yao, M., Tanaka, I., and Kumagai, I. (2004) Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: The case of Pyrococcus horikoshii CutA. FEBS Lett. 556, 167-174
44. Culotta, V.C., Joh, H.D., Lin, S.J., Slekar, K.H., and Strain, J. (1995) A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering. J. Biol. Chem. 270, 29991-29997
45. Jensen, L.T., Howard, W.R., Strain, J.J., Winge, D.R., and Culotta, V.C. (1996) Enhanced effectiveness of copper ion buffering by CUP1 metallothionein compared with CRS5 metallothionein in Saccharomyces cerevisiae. J. Biol. Chem. 271, 18514-18519
46. Culotta, V.C., Howard, W.R., and Liu, X.F. (1994) CRS5 encodes a metallothionein-like protein in Saccharomyces cerevisiae. J. Biol. Chem. 269, 25295-25302
47. Roosens, N.H., Bernard, C., Leplae, R., and Verbruggen, N. (2004) Evidence for copper homeostasis function of metallothionein (MT3) in the hyperaccumulator Thlaspi caerulescens. FEBS Lett. 577, 9-16
48. Clijsters, H. and Assche, F. (1985) Inhibition of photosynthesis by heavy metals. Photosynth. Res. 7, 31-40
49. Nielsen, H.D., Brownlee, C., Coelho, S.M., and Brown, M.T. (2003) Inter-population differences in inherited copper tolerance involve photosynthetic adaptation and exclusion mechanisms in Fucus serratus. New. Phytol. 160, 157-165
50. Cobine, P.A., Pierrel, F., and Winge, D.R. (2006) Copper trafficking to the mitochondrion and assembly of copper metalloenzymes. Biochim. Biophys. Acta 1763, 759-772
51. Mergeay, M. (1991) Towards an understanding of the genetics of bacterial metal resistance. Trends Biotechnol. 9, 17-24