HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Uldschmid, A. Articles by Marbach, K. Search for Related Content PubMed PubMed Citation Articles by Uldschmid, A. Articles by Marbach, K. Agricola Articles by Uldschmid, A. Articles by Marbach, K.

Identification and functional expression of ctaA, a P-type ATPase gene involved in copper trafficking in Trametes versicolor

Institute for Biochemistry, Ludwig Maximilians University of Munich, Feodor-Lynen-Str. 25, D-81377 Munich, Germany

Correspondence
Andreas Uldschmid
uldschmi{at}biochem.mpg.de

Here the identification and characterization of a gene encoding a copper-trafficking enzyme, ctaA (copper-transporting ATPase), from the basidiomycete Trametes versicolor 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 ctaA in yeast grown in the presence of copper led to a 15-fold increase in laccase yields, while overexpression of ctaA and tahA, a previously identified copper homeostasis gene of T. versicolor, was additive, leading to a 20-fold increase in laccase production. In T. versicolor, overexpression of ctaA and tahA 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 tahA and ctaA 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, tahA and ctaA 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.

The GenBank accession number for the Trametes versicolor ctaA gene sequence reported in this article is AY210894.

This article has been cited by other articles:

				L.-L. Kiiskinen, K. Kruus, M. Bailey, E. Ylosmaki, M. Siika-aho, and M. Saloheimo Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme Microbiology, September 1, 2004; 150(9): 3065 - 3074. [Abstract] [Full Text] [PDF]