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    Author(s): Luis F. Larrondo; Marcela Avila; Loreto Salas; Dan Cullen; Rafael Vicuna
    Date: 2003
    Source: Microbiology. Vol. 149 (2003): pages 1177-1182.
    Publication Series: Miscellaneous Publication
    PDF: View PDF  (174 KB)

    Description

    Analysis of genomic clones encoding a putative laccase in homokaryon strains of Ceriporiopsis subvermispora led to the identification of an allelic variant of the previously described lcs-1 gene. A cDNA clone corresponding to this gene was expressed in Aspergillus nidulans and in Aspergillus niger. Enzyme assays and Western blots showed that both hosts secreted active laccase. Relative to the isozymic forms of the native C. subvermispora enzyme, the A. niger-produced laccase had a higher molecular mass and gave a single band on IEF gels. In contrast, A. nidulans transformants secreted several isoforms remarkably similar to those of the native system. Considered together with previously reported Southern blots and protein sequencing, expression in A. nidulans supports the view that C. subvermispora 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, A. nidulans secretes apoprotein which can be reconstituted by a short incubation with Cu(I) and to a lesser extent with Cu(II).

    Publication Notes

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    • This article was written and prepared by U.S. Government employees on official time, and is therefore in the public domain.

    Citation

    Larrondo, Luis F.; Avila, Marcela; Salas, Loreto; Cullen, Dan; Vicuna, Rafael. 2003. Heterologous expression of laccase cDNA from Ceriporiopsis subvermispora yields copper-activated apoprotein and complex isoform patterns. Microbiology. Vol. 149 (2003): pages 1177-1182.

    Keywords

    Heterologous expression, laccase, molecular cloning, gene expression, fungi genetics, Ceriporiopsis subvermispora, Aspergillus niger, Aspergillus nidulans, enzymes, industrial applications, apoprotein, isoforms

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