Isolation of metallothionein genes and in silico structural characterization of their proteins Using molecular modeling from Yak (Bos grunniens)

Biochemical Genetics

Volumn 50, Issue 7-8, 2012, Pages 585-599

  Zhang, Liping ^a   Wu, Jianping ^a   Wang, Xinrong ^a   Liu, Bin ^a   Ma, Binyin ^a  

^a GANSU AGRICULTURAL UNIVERSITY   (China)

Author keywords

Metallothioneins (MTs); Molecular modeling; Structure function; Yak (Bos grunniens)

Indexed keywords

HEXAPEPTIDE; METALLOTHIONEIN; METALLOTHIONEIN I; METALLOTHIONEIN II; METALLOTHIONEIN III;

AMINO ACID SEQUENCE; ARTICLE; BIRD; BOS GRUNNIENS; COMPUTER MODEL; CONTROLLED STUDY; FISH; GENE; GENE INSERTION; GENE ISOLATION; GENETIC VARIABILITY; MAMMAL; METAL BINDING; METAL METABOLISM; METALLOTHIONEIN GENE; MOLECULAR EVOLUTION; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENY; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; SIMULATION; SPECIES DIFFERENCE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; SURFACE PROPERTY; YAK;

ADAPTATION, PHYSIOLOGICAL; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CATTLE; COMPUTATIONAL BIOLOGY; ENVIRONMENT; EVOLUTION, MOLECULAR; HUMANS; METALLOTHIONEIN; METALS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHYLOGENY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, NUCLEIC ACID;

BOS GRUNNIENS; MAMMALIA;

EID: 84865988176     PISSN: 00062928     EISSN: 15734927     Source Type: Journal    
DOI: 10.1007/s10528-012-9503-7     Document Type: Article

References (57)

1. Acarin L, Carrasco J, Gonzalez B, Hidalgo J, Castellano B (1999) Expression of growth inhibitory factor (metallothionein-III) mRNA and protein following excitotoxic immature brain injury. J Neuropathol Exp Neurol 58:389-397
2. Amiard JC, Amiard-Triquet C, Barka S, Pellerin J, Rainbow PS (2006) Metallothioneins in aquatic invertebrates: their role in metal detoxification and their use as biomarkers. Aquat Toxicol 76:160-202
3. Arnold K, Bordoli L, Kopp J, Schwede T (2006) The Swiss-Model workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195-201
4. Arseniev A, Schultze P, Worgotter E, Braun W, Wagner G, Vasak M, Kägi JHR, Wuthrich K (1988) Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. J Mol Biol 201:637-657
5. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE (2000) The protein data bank. Nucleic Acids Res 28:235-242
6. Braun W, Vaša'k M, Robbins AII, Stout CD, Wagner G, Kägi JHR, Wüthrich K (1992) Comparison of the NMR solution structure and the X-ray crystal structure of rat metallothionein-2. Proc Natl Acad Sci USA 89:10124-10128
7. Cai B, Zheng Q, Teng XC, Chen D, Wang Y, Wang KQ, Zhou GM, Xie Y, Zhang MJ, Sun HZ, Huang ZX (2006) The role of Thr5 in human neuron growth inhibitory factor. J Biol Inorg Chem 11:476-482
8. Cai B, Ding ZC, Zhang Q, Ni FY, Wang H, Zheng Q, Wang Y, Zhou GM, Wang KQ, Sun HZ, Wu HM, Huang ZX (2009) The structural and biological significance of the EAAEAE insert in the a-domain of human neuronal growth inhibitory factor. FEBS J 276:3547-3558
9. Carrasco J, Hernandez J, Gonzalez B, Campbell IL, Hidalgo J (1998) Localisation of metallothionein-I and -III expression in the CNS of transgenic mice with astrocyte-targeted expression of interleukin 6. Exp Neurol 153:184-194
10. Castrignanò T, De Meo PD, Cozzetto D, Talamo IG, Tramontano A (2006) The PMDB protein model database. Nucleic Acids Res 34:D306-D309
11. Chernaik ML, Huang PC (1991) Differential effect of cysteine-to-serine substitutions in metallothionein on cadmium resistance. Proc Natl Acad Sci USA 88:3024-3028
12. Chung RS, Holloway AF, Eckhardt BL, Harris JA, Vickers JC, Chuah M, West AK (2002) Sheep have an unusual variant of the brain-specific metallothionein, metallothionein-III. Biochem J 365:323-328
13. Cirelli C, Tononi G (2000) Gene expression in the brain across the sleep-walking cycle. Brain Res 885:303-321
14. Cismowski MJ, Narula SS, Armitage IM, Chernaik ML, Huang PC (1991) Mutation of invariant cysteines of mammalian metallothionein alters metal binding capacity, cadmium resistance, and 113Cd NMR spectrum. J Biol Chem 266:24390-24397
15. Cobbett C, Goldsbrough P (2002) Phytochelatins and metallothioneins: roles in heavy metal detoxification and homeostasis. Ann Rev Plant Biol 53:159-182
16. Coyle P, Philcox JC, Carey LC, Rofe AM (2002) Metallothione: the multipurpose F protein. Cell Mol Life Sci 59:627-647
17. Cuajungco MP, Lees GJ (1998) Nitric oxide generators produce accumulation of chelatable zinc in hippocampal neuronal perikarya. Brain Res 799:118-129
18. Erickson JC, Sewell AK, Jensen LT, Winge DR, Palmiter RD (1994) Enhanced neurotrophic activity in Alzheimer's disease cortex is not associated with down-regulation of metallothionein-III (GIF). Brain Res 649:297-304
19. Erickson JC, Hollopeter G, Thomas SA, Froelick GJ, Palmiter RD (1997) Disruption of the metallothionein-III gene in mice: analysis of brain zinc, behaviour, and neuron viability to metals, aging, and seizures. J Neuroscience 17:1271-1281
20. Faller P, Hasler DW, Zerbe O, Klauser S, Winge DR, Vaša'k M (1999) Evidence for a dynamic structure of human neuronal growth inhibitory factor and for major rearrangements of its metal-thiolate clusters. Biochemistry 38:10158-10167
21. Fowle D, Stillman MJ (1997) Comparison of the structures of the metal-thiolate binding site in Zn(II)-, Cd(II)-, and Hg(II)-metallothioneins using molecular modeling techniques. J Biomol Struct Dyn 14:393-406
22. Guex N, Peitsch MC (1997) Swiss-Model and the Swiss-dbViewer: an environment for comparative protein modelling. Electrophoresis 18:2714-2723
23. Hasler DW, Jensen LT, Zerbe O, Winge DR, Vasak M (2000) Effect of the two conserved prolines of human growth inhibitory factor (metallothionein-3) on its biological activity and structure fluctuation: comparison with a mutant protein. Biochemistry 39:14567-14575
24. Hess DT, Matsumoto A, Nudelman R, Stamler JS (2001) S-nitrosylation: spectrum and specificity. Nature Cell Biol 3:193-197
25. Hong SH, Maret WA (2003) A fluorescence resonance energy transfer sensor for the beta-domain of metallothionein. Proc Natl Acad Sci USA 100:2255-2260
26. Huang T, Wang P, Ye ZQ, Xu H, He Z, Feng KY, Hu L, Cui W, Wang K, Dong X, Xie L, Kong X, Cai YD, Li Y (2010) Prediction of deleterious non-synonymous SNPs based on protein interaction network and hybrid properties. PLoS ONE 5:e11900
27. Karotki AV, Vaša'k M (2009) Reaction of human metallothionein-3 with cisplatin and transplatin. J Biol Inorg Chem 14:1129-1138
28. Kopera E, Schwerdtle T, Hartwig A, Bal W (2004) Co(II) and Cd(II) substitute for Zn(II) in the zinc finger derived from the DNA repair protein XPA, demonstrating a variety of potential mechanisms of toxicity. Chem Res Toxicol 17:1452-1458
29. Margoshes M, Vallee BL (1957) A cadmium protein from equine imaging hyperintensity in Alzheimer's disease: correlation with kidney cortex. J Am Chem Soc 79:4813-4814
30. Meloni G, Faller P, Vaša'k M (2007) Redox silencing of copper in metal-linked neurodegenerative disorders: reaction of Zn7metallothionein-3 with Cu2? ions. J Biol Chem 282:16068-16078
31. Nordberg M, Nordberg GF (2000) Toxicological aspects of metallothionein. Cell Mol Biol Noisy-legrand 46:451-463
32. Oz G, Zangger K, Armitage IM (2001) Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: metallothionein-3. Biochemistry 40:11433-11441
33. Palmiter RD, Findley SD, Whitmore TE, Durnam DM (1992) MT-III, a brain specific member of the metallothionein gene family. Proc Natl Acad Sci USA 89:6333-6337
34. Rainbow PS, Phillips DJH (1993) Cosmopolitan biomonitors of trace metals. Mar Pollut Bull 26:593-601
35. Ramensky V, Bork P, Sunyaev S (2002) Human non-synonymous SNPs: server and survey. Nucleic Acids Res 30:3894-3900
36. Rechsteiner M, Rogers SW (1996) PEST sequences and regulation by proteolysis. Trends in Biochem Sci 21:267-271
37. Richards RI, Heguy A, Karin M (1984) Structural and functional analysis of the human metallothionein- 1A gene: differential induction by metal ions and glucocorticoids. Cell 37:263-272
38. Riek R, Prêcheur B, Wang Y, Mackay EA, Wider G, Güntert P, Liu A, Kägi JHR, Wüthrich K (1999) NMR structure of the sea urchin (Strangylocentrotus purpuratus) metallothionein MTA. J Mol Biol 291:417-428
39. Robbins AH, McRee DE, Williamson M, Collett SA, Xuong NH, Furey WF, Wang BC, Stout CD (1991) Refined crystal structure of Cd, Zn metallothionein at 2.0 A ° resolution. J Mol Biol 221:1269-1293
40. Roesijadi G (1996) Metallothionein and its role in toxic metal regulation. Comp Biochem Physiol Part C 113:117-123
41. Rogers S, Wells R, Rechsteiner M (1986) Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234:364-368
42. Romero-Isart N, Vaša'k M (2002) Advances in the structure and chemistry of metallothioneins. J Inorg Biochem 88:388-396
43. Romero-Isart N, Jensen LT, Zerbe O, Winge DR, Vaša'k M (2002) Engineering of metallothionein-3 neuroinhibitory activity into the inactive isoform metallothionein-1. J Biol Chem 277:37023-37028
44. Sambrook J, Russell D (2001) Molecular cloning: a laboratory manual, 3rd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
45. Schultze P, Worgotter E, Braun W, Wagner G, Väsa'k M, Kägi JHR, Wüthrich K (1988) Conformation of [Cd7]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy. J Mol Biol 203:251-268
46. Schwede T, Kopp J, Guex N, Peitsch MC (2003) Swiss-Model: an automated protein homology-modeling server. Nucleic Acids Res 31:3381-3385
47. Sewell AK, Jensen LT, Erickson JC, Palmiter RD, Winge DR (1995) Bioactivity of metallothionein-3 correlates with its novel betadomain sequence rather than metal-binding properties. Biochemistry 34:4740-4747
48. Stillman MJ (1995) Metallothioneins. Coord Chem Rev 144:461-511
49. Syring RA, Hoexum Brouwer T, Brouwer M (2000) Cloning and sequencing of cDNAs encoding for a novel copper-specific metallothionein and two cadmium-inducible metallothioneins from the blue crab Callinectes sapidus. Comp Biochem Physiol Part C 125:325-332
50. Uchida Y, Takio K, Titani K, Ihara Y, Tomonaga M (1991) The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein. Neuron 7:337-347
51. Vaša'k M, Hasler DW, Faller P (2000) metal-thiolate clusters in neuronal growth inhibitory factor (GIF). J Inorg Biochem 79:7-10
52. Wang Z, Moult J (2001) SNPs, protein structure, and disease. Hum Mutat 17:263-270
53. Williamson MP (1994) The structure and function of proline-rich regions in proteins. Biochem J 297:249-260
54. Wu JP, Ma BY, Ren HW, Zhang LP, Xiang Y, Brown MA (2007) Characterization of metallothioneins (MT-I and MT-II) in the yak. J Animal Sci 85:1357-1362
55. Wüthrich K (1991) Determination of the 3D structure of metallothioneins by nuclear magnetic resonance spectroscopy in solution. Methods Enzymol 205:502-520
56. Yamasaki F, Kurasaki M, Oikawa S, Emoto T, Okabe M, Kojima Y (1997) Effects of amino acid replacements on cadmium binding of metallothionein alpha-fragment. Cell Mol Life Sci 53:459-465
57. Yu WH, Lukiw WJ, Bergeron C, Niznik HB, Fraser PE (2001) Metallothionein III is reduced in Alzheimer's disease. Brain Res 894:37-45