Cuprodoxin

Prinz, Roswitha; Weser, Ulrich

doi:10.1016/0014-5793(75)80079-2

Cited by 37 publications

(13 citation statements)

References 25 publications

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“…Since Ag+, As3+, and Cd2+ induced a large amount of CIIIMT, Cu may be incorporated into the metalfree CIIIMT. Although the valency of Cu was not determined in this study, it may be present as Cu+ (Reese et al, 1988) as it is in class I and I1 MTs (Prinz and Weser, 1975;Suzuki and Maitani, 1981;Bordas et al, 1982). …”

Section: Discussionmentioning

confidence: 99%

The Composition of Metals Bound to Class III Metallothionein (Phytochelatin and Its Desglycyl Peptide) Induced by Various Metals in Root Cultures of Rubia tinctorum

et al. 1996

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The induction of phytochelatins (PCs) and their desglycyl peptides (both are referred to as class III metallothionein [CIIIMT]) by exposure to various metals (Ag+, As3+, As5+, CdZ+, Cuz+, Ca3+, HgZ+, ln3+, Ni2+, PbZ+, Pd2+, Se4+, and ZnZ+) and the metal composition in the ClllMTs were investigated in root cultures of Rubia tinctorum L. All of these metal species induced PCs to various degrees when analyzed by the postcolumn derivatization highperformance liquid chromatography method. The desglycyl peptides of PCs often were also present. However, only Ag, Cd, and Cu were bound to the ClllMTs that they induced when analyzed by the high-performance liquid chromatography-inductively coupled plasma-atomic emission spectrometry method. Cu was also bound to the ClllMTs induced by Ag+, As3+, and Cd2+. After Ag+ exposure, an Fe peak that may be of Fe-CIIIMT was also observed. However, most of the metal species studied were not bound to the ClllMTs that they induced. ~~~

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Section: Discussionmentioning

confidence: 99%

The Composition of Metals Bound to Class III Metallothionein (Phytochelatin and Its Desglycyl Peptide) Induced by Various Metals in Root Cultures of Rubia tinctorum

et al. 1996

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“…The protein is found in many cell types and is inducible by various metal ions (2)(3)(4)(5)(6)(7) and glucocorticoids (8,9). Two sequence variants exist in the vertebrates thus far studied, and both are inducible.…”

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confidence: 99%

Antigenicity of metallothionein.

Winge¹,

Garvey²

1983

Proc. Natl. Acad. Sci. U.S.A.

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The antigenic determinants of vertebrate metallothionein have been determined by a competitive-binding double-antibody radioimmunoassay to consist of two immunologically dominant regions in the NH2-terminal domain (residues 1-29). The COOH-terminal domain (residues 30-61) exhibited trivial immunoreactivity in competitive binding assays. The tryptic peptide encompassing residues Metallothionein is a 6,800-dalton metal-binding protein of unknown function isolated originally by Margoshes and Vallee (1). The protein is found in many cell types and is inducible by various metal ions (2-7) and glucocorticoids (8,9). Two sequence variants exist in the vertebrates thus far studied, and both are inducible. The protein is unusual in that it contains 32 mol % cysteine (20 of 61 residues in vertebrates), and all cysteine residues are involved in metal chelation (3,4,(10)(11)(12)(13)(14)(15)(16)(17)(18). Metallothionein has a stable tertiary conformation with the apoprotein being a random coil with possibly some short-range order (19,20). The structure appears to consist of two domains, each containing a metal-cysteine cage (21-23). Recently, Winge and Mildossy (24) showed that the two domains of Cd,Zn-thionein with seven metal atoms are separable by limited proteolysis. The COOH-terminal half of the molecule (residues 30-61) contained the four-metal atom-cysteine center (cluster A) and therefore the three-metal atom-cysteine center (cluster B) must be enfolded by the NH2-terminal half of the molecule (residues 1-29).With the isolated domains and peptide fragments of rat metallothionein available, we were interested in determining the immunoreactive properties of the domains and fragments in comparison with those of the native protein. (24). The a-fragments were prepared from both isoforms of metallothionein, designated Cd,Zn-MT-1 and Cd,Zn-MT-2. Purity of the a-peptides was assessed by amino acid analysis and NH2-terminal sequence analysis (24).The tryptic peptide OT1 (residues 1-25) was prepared by proteolysis of performic acid-oxidized thionein 2 with trypsin at a protease/thionein ratio (wt/wt) of 1:50 in 0.1 M pyridine acetate (pH 5) at 37°C for 48 hr. The tryptic peptides were resolved by gel filtration on a Sephadex G-50 column (1.5 X 160 cm) equilibrated with 1 M acetic acid as described by Huang et al. (15). The effluent fractions (1.5 m per tube) were monitored by the fluorescamine reaction after alkaline hydrolysis. The fluorescence emission at 475 nm was monitored in a Perkin-Elmer 650-10S spectrophotometer with excitation at 390 nm. The peptide eluting first was shown to be tryptic peptide OT1, in that its amino acid composition was the same as that for OTl reported by Huang et al. (16) (Table 1).Modification Reactions. Metallothionein was modified by incubation with 30% H202/88% formic acid, 1:9 (vol/vol), for 4 hr at 4°C (27). The cysteine -* cysteic acid conversion yield was 70-85%. Thionein was carboxymethylated by treatment with iodoacetate in 6 M guanidine HCI/l mM EDTA/0.1 M Tris HCl, pH 8....

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“…The locus copy number was also positively correlated with the copper resistance level of a given strain and with the production level of a low molecular weight copper binding protein. We determined the full nucleotide sequence of the CUPJ locus and established that the basic amplification unit contains a copper-regulated transcription unit encoding a low molecular weight, cysteine-rich protein-copper chelatin (25)(26)(27). The sequence of this protein bears some resemblance to the more familiar heavy metal binding protein-metallothionein (28)-which is responsible for protecting mammalian cells against the toxic effects of cadmium ions (29,30).…”

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confidence: 99%