Copper metallothionein, a copper-binding protein from Neurospora crassa
- 1 March 1980
- journal article
- Published by Springer Nature in Nature
- Vol. 284 (5754), 368-370
- https://doi.org/10.1038/284368a0
Abstract
Copper is an essential constituent of many proteins which participate in biologically important reactions. In contrast to iron, where different metal storage and transport proteins have been extensively characterised, the existence of copper proteins serving such functions is still a matter of controversy. Studies on the biosynthesis of tyrosinase from Neurospora crassa with respect to the copper status of this fungus have shown that this organism accumulates copper with the concomitant synthesis of a small molecular weight copper-binding protein. This protein is now shown to have a striking sequence homology to the zinc- and cadmium-containing metallothioneins from vertebrates. Growth experiments suggest that this molecule fulfills several important physiological functions in this organism such as copper storage, copper detoxification and provision of copper for tyrosinase.Keywords
This publication has 14 references indexed in Scilit:
- MetallothioneinTrends in Biochemical Sciences, 1978
- Copper-thionein from fetal bovine liverBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- Copper and iron metalloproteinsTrends in Biochemical Sciences, 1976
- Isolation of (copper, zinc-) thioneins from pig liverBiochemical Journal, 1976
- Purification of low molecular weight copper proteins from copper loaded liverBiochemical and Biophysical Research Communications, 1975
- Copper-chelatin: Isolation from various eucaryotic sourcesArchives of Biochemistry and Biophysics, 1975
- Copper-chelatin: Purification and properties of a copper-binding protein from rat liverArchives of Biochemistry and Biophysics, 1975
- A Naturally Occurring Cu-Thionein inSaccharomyces cerevisiaeHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1975
- The Chromatographic Determination of Cystine and Cysteine Residues in Proteins as S-β-(4-Pyridylethyl)cysteineJournal of Biological Chemistry, 1970
- [33] S-AminoethylationPublished by Elsevier ,1967