1887

Abstract

Here the identification and characterization of a gene encoding a copper-trafficking enzyme, (opper-ransporting TPase), from the basidiomycete are described. This P-type copper ATPase gene has two alleles, differing primarily in the length of the second, unusually long intron, and encodes a 983 aa protein with 40 % sequence identity to yeast Ccc2p. Overexpression of in yeast grown in the presence of copper led to a 15-fold increase in laccase yields, while overexpression of and , a previously identified copper homeostasis gene of . , was additive, leading to a 20-fold increase in laccase production. In . , overexpression of and led to an eightfold increase in laccase expression, and a cotransformant still expressed laccase at 3000 μM copper when hardly any laccase activity is detected in the wild-type strain. Apparently, at low to moderate levels of copper and overexpression disturbs the normal hierarchy of copper distribution, resulting in more being directed to the Golgi, while with high copper amounts that normally switch on the copper detoxification processes, and gene products seem to out-compete the metallothionein copper chaperones, meaning laccase is still supplied with copper. These results may lead to a better understanding of copper trafficking and the hierarchy of copper distribution in the cell, and possibly be useful for constructing laccase-overproducing strains for biotechnological purposes.

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2003-08-01
2020-04-07
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