Cloning and transcript analysis of type 2 metallothionein gene (SbMT-2) from extreme halophyte Salicornia brachiata and its heterologous expression in E. coli

Gene

Volumn 499, Issue 2, 2012, Pages 280-287

  Chaturvedi, Amit Kumar ^a   Mishra, Avinash ^a   Tiwari, Vivekanand ^a   Jha, Bhavanath ^a  

^a CSIR CENTRAL SALT AND MARINE CHEMICALS RESEARCH INSTITUTE   (India)

Author keywords

Abiotic stress; GST fusion protein; Heavy metals; Metal binding; Metal toxicity; Phytoremediation

Indexed keywords

CADMIUM; COPPER; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; METALLOTHIONEIN II; SODIUM CHLORIDE; ZINC;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; DETOXIFICATION; DOWN REGULATION; DROUGHT STRESS; ESCHERICHIA COLI; GENE ISOLATION; HALOPHYTE; HEAT; HOMEOSTASIS; METAL BINDING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN ISOLATION; REAL TIME POLYMERASE CHAIN REACTION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SALICORNIA BRACHIATA; SOUTHERN BLOTTING; UPREGULATION;

AMINO ACID SEQUENCE; CHENOPODIACEAE; CLONING, MOLECULAR; ESCHERICHIA COLI; GENE EXPRESSION; METALLOTHIONEIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; SALT-TOLERANT PLANTS;

SALICORNIA BRACHIATA;

EID: 84860241983     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2012.03.001     Document Type: Article

References (59)

1. Altschul S.F., et al. Protein database searches using compositionally adjusted substitution matrices. FEBS J. 2005, 272:5101-5109.
2. Andrews G.K. Regulation of metallothionein gene expression by oxidative stress and metal ions. Biochem. Pharmacol. 2000, 59:95-104.
3. Bilecen K., et al. Triticum durum metallothionein: isolation of the gene and structural characterization of the protein using solution scattering and molecular modeling. J. Biol. Chem. 2005, 280:13701-13711.
4. Blindauer C.A., Leszczyszyn O.I. Metallothioneins: unparalleled diversity in structures and functions for metal ion homeostasis and more. Nat. Prod. Rep. 2010, 27:720-741.
5. Blindauer C.A., Schmid R. Cytosolic metal handling in plants: determinants for zinc specificity in metal transporters and metallothioneins. Metallomics 2010, 2:510-529.
6. Bradford M.M. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
7. Bratić A.M., Majić D.B., Samardžć J.T., Maksimović V.R. Functional analysis of the buckwheat metallothionein promoter: tissue specificity pattern and up-regulation under complex stress stimuli. J. Plant Physiol. 2009, 166:996-1000.
8. Chang T., Liu X., Xu H., Meng K., Chen S., Zhu Z. A metallothionein-like gene htMT2 strongly expressed in internodes and nodes of Helianthus tuberosus and effects of metal ion treatment on its expression. Planta 2004, 218:449-455.
9. Cherian G.M., Chan H.M. Biological functions of metallothioneins-a review. Metallothioneins III: biological roles and medical implications 1993, 87-109. Birkhäuser, Basel. K.T. Suzuki, N. Imura, M. Kimura (Eds.).
10. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 1987, 162:156-159.
11. Cobbett C., Goldsbrough P. Phytochelatins and metallothioneins: roles in heavy metal detoxification and homeostasis. Annu. Rev. Plant Biol. 2002, 53:159-182.
12. Domènech J., Mir G., Huguet G., Capdevila M., Molinas M., Atrian S. Plant metallothionein domains: functional insight into physiological metal binding and protein folding. Biochimie 2006, 88:583-593.
13. (II)-binding abilities of recombinant Quercus suber metallothionein, QsMT: bridging the gap between phytochelatins and metallothioneins. J. Biol. Inorg. Chem. 2007, 12:867-882.
14. Dondero F., Cavaletto M., Ghezzi A.R., Terza A.L., Banni M., Viarengo A. Biochemical characterization and quantitative gene expression analysis of the multi stress inducible metallothionein from Tetrahymena thermophila. Protist 2004, 155:157-168.
15. Evans K.M., Gatehouse J.A., Lindsay W.P., Shi J., Tommey A.M., Robinson N.J. Expression of the pea metallothionein-like gene PsMTA in Escherichia coli and Arabidopsis thaliana and analysis of trace metal ion accumulation: Implications for PsMTA function. Plant Mol. Biol. 1992, 20:1019-1028.
16. Finn R.D., et al. Pfam: clans, web tools and services. Nucleic Acids Res. 2006, 34:D247-D251.
17. Fowler B.A., Hildebrand C.E., Kojima Y., Webb M. Nomenclature of metallothioneins. Metallothionein II 1987, 19-22. Birhäuser Verlag, Basel. J.H.R. Kägi, Y. Kojima (Eds.).
18. Freisinger E. Plant MTs-long neglected members of the metallothionein superfamily. Dalton Trans. 2008, 47:6663-6675.
19. Freisinger E. Metallothioneins in plants. Metal Ions in Life Sciences: Metallothioneins and Related Chelators vol. 5 2009, 107-153. Royal Society of Chemistry, Cambridge. A. Sigel, H. Sigel, R.K.O. Sigel (Eds.).
20. Freisinger E. Structural features specific to plant metallothioneins. J. Biol. Inorg. Chem. 2011, 16:1035-1045.
21. Gasteiger E., et al. Protein identification and analysis tools on the expasy server. The Proteomics Protocols Handbook 2005, 571-607. Humana Press, USA. J.M. Walker (Ed.).
22. Gonzalez-Mendoza D., Moreno A.Q., Zapata-Perez O. Coordinated responses of phytochelatin synthase and metallothionein genes in black mangrove, Avicennia germinans, exposed to cadmium and copper. Aquat. Toxicol. 2007, 83:306-314.
23. Guo W.J., Meetam M., Goldsbrough P.B. Examining the specific contributions of individual Arabidopsis metallothioneins to copper distribution and metal tolerance. Plant Physiol. 2008, 146:1697-1706.
24. Hassinen V.H., Tuomainen M., Peräniemi S., Schat H., Kärenlampi S.O., Tervahauta A.I. Metallothioneins 2 and 3 contribute to the metal-adapted phenotype but are not directly linked to Zn accumulation in the metal hyperaccumulator, Thlaspi caerulescens. J. Exp. Bot. 2009, 60:187-196.
25. Huang G.Y., Wang Y.S. Expression analysis of type 2 metallothionein gene in mangrove species (Bruguiera gymnorrhiza) under heavy metal stress. Chemosphere 2009, 77:1026-1029.
26. Huang G.Y., Wang Y.S. Expression and characterization analysis of type 2 metallothionein from grey mangrove species (Avicennia marina) in response to metal stress. Aquat. Toxicol. 2010, 99:86-92.
27. Hussain S., Slikker W., Syed F.A. Role of metallothionein and other antioxidants in scavenging superoxide radicals and their possible role in neuroprotection. Neurochem. Int. 1996, 29:145-152.
28. Jha B., Agarwal P.K., Reddy P.S., Lal S., Sopory S.K., Reddy M.K. Identification of salt -induced genes from Salicornia brachiata, an extreme halophyte through expressed sequence tags analysis. Genes Genet. Syst. 2009, 84:111-120.
29. Jha B., Sharma A., Mishra A. Expression of SbGSTU (tau class glutathione S-transferase) gene isolated from Salicornia brachiata in tobacco for salt tolerance. Mol. Biol. Rep. 2011, 38:4823-4832.
30. Jin S., Cheng Y., Guan Q., Liu D., Takano T., Liu S. A metallothionein-like protein of rice (rgMT) functions in E. coli and its gene expression is induced by abiotic stresses. Biotechnol. Lett. 2006, 28:1749-1753.
31. Kholodova V., Volkov K., Kuznetsov V. Plants under heavy metal stress in saline environments. Soil Heavy Metals, Soil Biology 2010, vol. 19:163-183. Springer, Berlin Heidelberg. I. Sherameti, A. Varma (Eds.).
32. Kille P., Winge D.R., Harwood J.L., Kay J. A plant metallothionein produced in E. coli. FEBS Lett. 1991, 295:171-175.
33. Klaassen C.D., Liu J., Choudhuri S. Metallothionein: an intracellular protein to protect against cadmium toxicity. Annu. Rev. Pharmacol. Toxicol. 1999, 39:267-294.
34. T method. Methods 2001, 25:402-408.
35. c-1: the second part of the puzzle. J. Biol. Inorg. Chem. 2011, 16:683-694.
36. Macfarlane G.R., Burchett M.D. Photosynthetic pigments and peroxidase activity as indicators of heavy metal stress in the grey mangrove, Avicennia marina (Forsk.)-Vierh. Mar. Pollut. Bull. 2001, 42:233-240.
37. Marchler-Bauer A., et al. CDD: specific functional annotation with the conserved domain database. Nucleic Acids Res. 2009, 37:205-210.
38. McGuffin L.J., Bryson K., Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 2000, 16:404-405.
39. Mir G., et al. A plant type 2 metallothionein (MT) from cork tissue responds to oxidative stress. J. Exp. Bot. 2004, 55:2483-2493.
40. Murashige T., Skoog F. A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol. Plant. 1962, 15:431-497.
41. Perkins D.N., Pappin D.J.C., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
42. c-1 metallothionein: a metal-binding domain with a distinctive structure. J. Mol. Biol. 2009, 387:207-218.
43. Pilon-Smits E.A.H., Zhu Y.L., Sears T., Terry N. Overexpression of glutathione reductase in Brassica juncea: effects on cadmium accumulation and tolerance. Physiol. Plant. 2000, 110:455-460.
44. Quevillon E., et al. InterProScan: protein domains identifier. Nucleic Acids Res. 2005, 33:W116-W120.
45. Robinson N.J., Tommey A.M., Kuske C., Jackson P.J. Plant metallothioneins. Biochem. J. 1993, 295:1-10.
46. Roosens N.H., Leplae R., Bernard C., Verbruggen N. Variations in plant metallothioneins: the heavy metal hyperaccumulator Thlaspi caerulescens as a study case. Planta 2005, 222:716-729.
47. Sambrook J., Russell D.W. Molecular Cloning: a Laboratory Manual 2001, Cold Spring Harbor Laboratory Press, New York. third ed.
48. T method. Nat. Protoc. 2008, 3:1101-1108.
49. Sekhar K., Priyanka B., Reddy V.D., Rao K.V. Metallothionein 1 (CcMT1) of pigeonpea (Cajanus cajan, L.) confers enhanced tolerance to copper and cadmium in Escherichia coli and Arabidopsis thaliana. Environ. Exp. Bot. 2011, 72:131-139.
50. Sharma A., Gontia I., Agarwal P.K., Jha B. Accumulation of heavy metals and its biochemical responses in Salicornia brachiata, an extreme halophyte. Mar. Biol. Res. 2010, 6-5:511-518.
51. Singh R.K., Anandhan S., Singh S., Patade V.Y., Ahmed Z., Pande V. Metallothionein-like gene from Cicer microphyllum is regulated by multiple abiotic stresses. Protoplasma 2011, 248:839-847.
52. Song Y.Z., Li P.P., Du Y.J. Expression and functional analysis of BjMT-2, a metallothionein type-2 from Brassica juncea, in E. coli. Adv. Mater. Res. 2011, 183-185:65.
53. Tommey A.M., Shi J., Lindsay W.P., Urwin P.E., Robinson N.J. Expression of the pea gene PsMTA in E. coli: metal-binding properties of the expressed protein. FEBS Lett. 1991, 292:48-52.
54. Usha B., Prashanth S.R., Parida A. Differential expression of two metallothionein encoding genes during heavy metal stress in the mangrove species, Avicennia marina (Forsk.) Vierh. Curr. Sci. 2007, 93:1215-1219.
55. Usha B., Venkataraman G., Parida A. Heavy metal and abiotic stress inducible metallothionein isoforms from Prosopis juliflora (SW) D.C. show differences in binding to heavy metals in vitro. Mol. Genet. Genomics 2009, 281:99-108.
56. Valle B.L., Maret W. The functional potential and potential functions of metallothioneins: a personal perspective. Metallothioneins III: Biological Roles and Medical Implications 1993, 1-27. Birkhäuser, Basel. K.T. Suzuki, N. Imura, M. Kimura (Eds.).
57. Zhou G.K., Xu Y.F., Liu J.Y. Characterization of a rice class II metallothionein gene: tissue expression patterns and induction in response to abiotic factors. J. Plant Physiol. 2005, 162:686-696.
58. Zhu Y.L., Pilon-Smits E.A.H., Jouanin L., Terry N. Overexpression of glutathione synthetase in Indian mustard enhances cadmium accumulation and tolerance. Plant Physiol. 1999, 119:73-80.
59. 2 stress. Plant Physiol. Biochem. 2010, 48:710-715.