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Copper metallothionein, a copper-binding protein from Neurospora crassa
Copper is an essential constituent of many proteins which participate in biologically important reactions 1 . 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 co...
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Published in: | Nature (London) 1980-03, Vol.284 (5754), p.368-370 |
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Main Author: | |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Copper is an essential constituent of many proteins which participate in biologically important reactions
1
. 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
2–8
. 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
9
. 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. |
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ISSN: | 0028-0836 1476-4687 |
DOI: | 10.1038/284368a0 |