Genetic Design of Stable Metal-Binding Biomolecules, Oligomeric Metallothioneins

References

• Beach L. R., Palmiter R. D. “Amplification of the metallothionein-I gene in cadmium-resistant mouse cells”. Proc. Natl. Acad. Sci. USA 1981; 78: 2110–2114
   PubMed Web of Science ®Google Scholar
• Berka T., Shatzman A., Zimmerman J., Strickler J., Rosenberg M. “Efficient expression of the yeast metallothionein gene in Escherichia coli”. J. Bacteriol 1988; 170: 21–26
   PubMed Web of Science ®Google Scholar
• Brady F. O. “The physiological function of metallothionein”. Trends Biochem. Sci 1982; 7: 143–145
   Web of Science ®Google Scholar
• Churbatsu L. S., Meneghini R. “Metallothionein protects DNA from oxidative damage”. Biochem. J 1993; 291: 193–198
   PubMed Web of Science ®Google Scholar
• Feldman S. L., Cousins RJ. “Degradation of hepatic zinc-thionein afterparental zinc administration”. Biochem. J 1976; 160: 583–588
   PubMed Web of Science ®Google Scholar
• Hong S.-H., Tokayama M, Maret W., Murooka Y. “High yield expression and single step purification of human thioneim/metallothioneim”. Protein Exp. Purif. 2001; 21: 243–250
   PubMed Web of Science ®Google Scholar
• Hou Y.-M., Kim R., Kim S. H. “Expression of the mouse metallothionein-I gene in Escherichia coli: increased tolerance to heavy metals”. Biochem. Biophys. Acta 1988; 951: 230–234
   PubMedGoogle Scholar
• Jacob Maret C. W., Vallee B. L. “Control of zinc transfer between thionein, metallothionein, and zinc proteins”. Proc. Natl. Acad. Sci. USA 1998; 95: 3489–3494
   PubMed Web of Science ®Google Scholar
• Kågi J. H.R., Schåffer A. “Biochemistry of metallothionein”. Biochemistry 1988; 27: 8509–8511
   PubMed Web of Science ®Google Scholar
• Kågi J. H.R., Himmelhoch S. R., Whanger P. D., Bethune J. L., Vallee B. L. “Equine hepatic and neural metallothioneins. Purification, molecular weight, amino acid composition, and metal content”. J. Biol Chem 1974; 249: 3537–3542
   PubMed Web of Science ®Google Scholar
• Kille P., Stephens P., Cryer A., Kay J. “The expression of a synthetic rainbow trout metallothionein gene”. Biochem. Biophys. Acta 1990; 1048: 578–586
   Google Scholar
• Krezoski S., Villalobos J., Shaw C. F., III, Petering D. H., III. “Kinetic liability of zinc bound to metallothionein in Ehrlich cells”. Biochem. J 1998; 255: 483–491
   Google Scholar
• Kull F. J., Reed H. F., Elgren T. E., Ciardelli T. L., Wilcox D. E. “Solid-phase peptide synthesis of the α and β domains of liver metallothionein 2 and the metallothionein of Neurospora crassa”. J. Am. Chem. Soc. 1990; 112: 2291–2298
   Web of Science ®Google Scholar
• Ljungcrantz P. “Construction of an artificial bifunctional enzyme, beta-galactosidase/galactose dehydrogenase, exhibiting efficient galactose channeling”. Biochemistry 1989; 28: 8786–8792
   PubMed Web of Science ®Google Scholar
• Maniatis T. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbour, NY 1982
   Google Scholar
• Margoshes M., Vallee B. L. “A cadmium protein from equine kidney cortex”. J. Am. Chem. Soc 1957; 79: 4813–4814
   Web of Science ®Google Scholar
• Murooka Y., Arnheiter H. “Expression of the vesicular stomatis virus nucleocapsid protein by the lambda PR and PL promoters in Escherichia coli“. J. Biotechnol 1985; 2: 289–301
   Web of Science ®Google Scholar
• Murooka Y., Mitani I. “Efficient expression of a promoter-controlled gene: tandem promoters of lambda PR and PL functional in enteric bacteria”. J. Biotechnol 1985; 2: 303–316
   Web of Science ®Google Scholar
• Murooka Y., Nagaoka T. “Expression of cloned monkey metallothionein in Escherichia coli“. Appl. Environ. Microbiol 1987; 53: 204–207
   PubMed Web of Science ®Google Scholar
• Nemer M., Travaglini E. C., Rondinelli E., D'Alonzo J. “Developmental regulation, induction, and embrionic tissue specificity of sea urchin metallothionein gene expression”. Dev. Biol 1984; 102: 471–482
   PubMed Web of Science ®Google Scholar
• Odawara F., Kurasaki M., Suzuki-Kurasaki M., Oikawa S., Emoto T., Yamasaki F., Linde Arias A. R., Kojima Y. “Expression of human metallothionein-2 in Escherichia coli: cadmium tolerance of transformed cells”. J. Biochem 1995; 118: 1131–1137
   PubMed Web of Science ®Google Scholar
• Ohta N., Okada Y., Tanaka K. “Amino acids and peptides. VIII. Synthesis of a hexacosapeptide corresponding to the C-terminal sequence 36–61 of human metallothionein II (MTII) and determination of its heavy metal binding activity”. Chem. Pharm. Bull 1983; 31: 1885–1895
   PubMed Web of Science ®Google Scholar
• Okada Ohta Y. N., Yagyu M., Min K. S., Onosaka S., Tanaka K. “Synthesis of nanocosapeptide (β-fragment) corresponding to the N-terminal sequence 1–29 of human liver metallothionein II and its heavy metal-binding properties”. FEBS Lett 1985; 183: 375–378
   PubMed Web of Science ®Google Scholar
• Otvos J. D., Engeseth H. R., Nettesheim D. G., Hilt C. R. “Interprotein metal exchange reactions of metallothionein”. Exp. Suppl 1987; 52: 171–178
   PubMedGoogle Scholar
• Pederson A. O., Jacobson J. “Reactivity of the thiol group in human and bovine albumin at pH 3–9. as measured by exchange with 2.2′-dithiodipyridine”. Eur, J. Biochem 1980; 106: 291–295
   PubMedGoogle Scholar
• Saito S., Hunziker RE. “Differential sensitivity of metallothionein-I and -II in liver of zinc-injected rat toward proteolysis”. Biochem. Biophys. Acta 1996; 1289: 65–70
   PubMed Web of Science ®Google Scholar
• Stark M. J.R. “Multicopy expression vectors carrying the lac repressor gene for regulated high-level expression of genes in Escherichia coli”. Gene 1987; 51: 255–267
   PubMed Web of Science ®Google Scholar
• Vasák M., Kågi J. H.R., Hill H. A.O. “Zinc (II). cadmium (II), and mercury (II) thiolate transition in metallothionein”. Biochemistry 1981; 20: 2852–2856
   PubMed Web of Science ®Google Scholar
• Wright Mc C. F., Kenny K., Hamer D. H., Byrd J., Winge D. R. “Structural and functional studies of the amino terminus of yeast metallothionein”. J. Biol. Chem 1987; 262: 12912–12919
   PubMed Web of Science ®Google Scholar
• Xiong Y., Ru B. “Purification and characteristics of recombinant mouse metallothionein-I from Escherichia coli“. J. Biochem 1997; 121: 1102–1106
   PubMed Web of Science ®Google Scholar
• Yamashita M., Kuwata H., Murakami H., Murooka Y. “Genetic design of a gene for human metallothionein II and its expression as an active fusion protein in Escherichia coli“. J. Ferment. Bioeng 1994; 77: 113–118
   Google Scholar
• Yanish-Perron C, Vierra J., Messing J. “Improved M13 phage cloning vectors and host strains: nucleotide sequences of M13mp18 and pUC19 vectors”. Gene 1985; 33: 103–119
   PubMed Web of Science ®Google Scholar