Umecyanin, a novel intensely blue copper protein from horseradish root

Paul, K. G.; Stigbrand, Torgny

doi:10.1016/0005-2795(70)90265-5

Cited by 38 publications

(14 citation statements)

References 30 publications

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“…(2) umecyanin from horseradish roots (Armoracia laphutifolia) (Van Driessche et al, 1995); and (3) a gene product (BCB) predicted from the nucleotide sequence of a negatively light-regulated gene isolated from Arabidopsis thaliana (Van Gysel et al, 1993). Although umecyanin and cucumber stellacyanin were isolated originally in 1970 and 1979, respectively, their amino acid sequences became available only recently (Paul & Stigbrand. 1970;Aikazyan & Nalbandyan, 1979).…”

Section: Comparative Analysis Of Stellacyanins From Four Different Somentioning

confidence: 99%

Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form

et al. 1996

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The cDNA encoding the 182 amino acid long precursor stellacyanin from Cucumis sariwus was isolated and characterized. The protein precursor consists of four sequence domains: I, a 23 amino acid hydrophobic N-terminal signal peptide with features characteristic of secretory proteins; 11, a 109 amino acid copper-binding domain; 111, a 26 amino acid hydroxyproline-and serine-rich peptide characteristic of motifs found in the extensin family, extracellular structural glycoproteins found in plant cell walls; and IV, a 22 amino acid hydrophobic extension. Maturation of the protein involves posttranslational processing of domains I and IV. The copper-binding domain (domain 11), which shares high sequence identity with other stellacyanins, has been expressed without its carbohydrate attachment sites, refolded from the Escherichia coli inclusion bodies, purified, and characterized by electronic absorption, EPR, ESEEM, and RR spectroscopy. Its spectroscopic properties are nearly identical to those of stellacyanin from the Japanese lacquer tree Rhus verniciferu, the most extensively studied and best characterized stellacyanin, indicating that this domain folds correctly, even in the absence of its carbohydrate moiety. The presence of a hydroxyproline-and serine-rich domain I11 suggests that stellacyanin may have a function other than that of a diffusible electron transfer protein, conceivably participating in redox reactions localized at the plant cell wall, which are known to occur in response to wounding or infection of the plant.

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Section: Comparative Analysis Of Stellacyanins From Four Different Somentioning

confidence: 99%

Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form

et al. 1996

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“…In any case, considering the molecular properties determined for purified fraction II, it is clear that this is not a metallothionein-like protein or thiol-rich metal-binding protein (Dunn et al 1987;Schultz and Hutchinson 1988) and is not similar to other low-molecular-weight copper-proteins involved in metal tolerance which have been purified from plants ( Robinson and Jackson 1986;Grill etal. Fraction II could perhaps be another small blue protein similar to umecyanin or stellacyanin which have a similar molecular weight and also contain 1 Cu-atom per molecule (Paul and Stigbrand 1970;Walker and Webb 1981) though this still has to be demonstrated. Fraction II could perhaps be another small blue protein similar to umecyanin or stellacyanin which have a similar molecular weight and also contain 1 Cu-atom per molecule (Paul and Stigbrand 1970;Walker and Webb 1981) though this still has to be demonstrated.…”

Section: Discussionmentioning

confidence: 99%

Copper-binding proteins and copper tolerance in Pisam sativum L.

Palma

Yáñez

Gómez

et al. 1990

Planta

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The effect of high nutrient levels of copper on the low-molecular-weight copper-proteins of leaves from plants of two cultivars of Pisum sativum L., with different sensitivity to copper, was investigated. Gel-filtration chromatography of leaf extracts from Cu-tolerant and Cu-sensitive plants grown with 1 μM Cu(II), showed the presence of only two copper peaks (I and II), but growth of plants with 240 μM Cu(II) induced two additional copper fractions (III and IV). Fractions II and III were purified by solvent extraction, gel-filtration and ion-exchange chromatography, and their molecular weights, subunit sizes, absorption spectra, metalprotein stoichiometry and amino-acid contents were determined. Fraction II was a polypeptide of Mr 15000 composed of a single chain. The purification of fraction III produced a copper-containing fraction (III-1) of Mr 3700, and a copper-protein (III-2) with an Mr, by sodium dodecyl sulfate-urea-polyacrylamide gel electrophoresis, of 66000. The metal contents of fractions III-1 and III-2 were higher in Cu-tolerant than in Cu-sensitive plants. On the basis of amino-acid analyses, fraction III-1 appeared to be complexes of Cu(II)-poly-isoleucine and Cu(II)-poly-leucine. The results rule out the existence, in pea leaves, of any protein similar to either animal metallothioneins or to any of the low-molecularweight metal-binding proteins or peptides described in other plants and reported to be involved in metal tolerance. In the mechanism of copper tolerance at the leaf level, fractions III-1 (Mr 3700), III-2 (Mr 66000), and IV (Mr 2000) appear to have a role, fraction IV being specifically induced in the tolerant cultivar by Cu(II). Fractions III-1 and III-2 could participate in a different mechanism, adaptive in character, involving an enhanced capacity to bind copper in Cu-tolerant plants.

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“…As said earlier, the physiological role of umecyanin is not yet known. The protein was isolated as a co-product during the isolation of peroxidase from the peelings of horseradish roots (Paul & Stigbrand, 1970). Because two of the three cysteines in umecyanin are linked in a disulfide bridge, whereas the third acts as one of the four copper ligands, it is likely that the association rather occurs through hydrophobic interaction.…”

Section: Evolutionary Position Of Umecyaninmentioning

confidence: 99%

“…Because two of the three cysteines in umecyanin are linked in a disulfide bridge, whereas the third acts as one of the four copper ligands, it is likely that the association rather occurs through hydrophobic interaction. Umecyanin cannot replace laccase in the reduction of oxygen by ascorbic acid (Paul & Stigbrand, 1970), but like other small blue copper proteins, it can be used as an electron donor instead of vitamin C if laccase is present (Stigbrand, 1971).…”

Section: Evolutionary Position Of Umecyaninmentioning

confidence: 99%

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Heterogeneity of the covalent structure of the blue copper protein umecyanin from horseradish roots

et al. 1995

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The covalent structure of umecyanin has been determined by a combination of classical Edman degradation sequence analysis and plasma desorption, laser desorption, and electrospray ionization mass spectrometry. The preparation appeared to contain two isoforms having either a valine (75%) or an isoleucine (25%) residue at position 48. The polypeptide chain of 115 amino acids is strongly heterogeneous at its C-terminal end as a result of proteolytic cleavages at several places within the last 10 residues. The major fraction of the umecyanin preparation is only 106 residues long. The C-terminal tail 107-115 contains mainly alanine and glycine residues and a single hydroxyproline residue. In the native protein there is a disulfide bridge between Cys 91 and Cys 57, but in the apoprotein there is a disulfide shift that involves Cys 91 and one of the four copper binding residues (Cys 85). The three other ligand binding residues are His 44, His 90, and Gln 95. This tetrad of amino acids is the same as occurs in other type 1 copper proteins from plants such as cucumber peeling cupredoxin and lacquer tree stellacyanin. The umecyanin isoforms are glycoproteins with a glycan core having the same carbohydrate composition as that of horseradish peroxidase, a fact that is convincingly supported thanks to the high accuracy of the electrospray mass spectrometric technique. We suggest that the glycan may play a role in the association of the protein to the cellular membrane, but the precise functional role of umecyanin remains to be determined. We also discuss the evolutionary position of umecyanin in relation to the type 1 copper proteins in general.

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Umecyanin, a novel intensely blue copper protein from horseradish root

Cited by 38 publications

References 30 publications

Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form

Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form

Copper-binding proteins and copper tolerance in Pisam sativum L.

Heterogeneity of the covalent structure of the blue copper protein umecyanin from horseradish roots

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