1887

Abstract

Analysis of genomic clones encoding a putative laccase in homokaryon strains of led to the identification of an allelic variant of the previously described gene. A cDNA clone corresponding to this gene was expressed in and in . Enzyme assays and Western blots showed that both hosts secreted active laccase. Relative to the isozymic forms of the native enzyme, the -produced laccase had a higher molecular mass and gave a single band on IEF gels. In contrast, transformants secreted several isoforms remarkably similar to those of the native system. Considered together with previously reported Southern blots and protein sequencing, expression in supports the view that has a single laccase gene and that multiple isoforms result from post-translational processes. In addition, several lines of evidence strongly suggest that under copper limitation, secretes apoprotein which can be reconstituted by a short incubation with Cu(I) and to a lesser extent with Cu(II).

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2003-05-01
2024-04-26
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