LYS2 gene and its mutation in Kluyveromyces lactis |
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Authors: | Alberti Adriana Ferrero Iliana Lodi Tiziana |
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Affiliation: | Dipartimento di Genetica Antropologia Evoluzione, University of Parma, Italy. |
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Abstract: | The KlLYS2 gene, encoding the alpha-aminoadipate reductase of Kluyveromyces lactis, was isolated by complementation of a lysA1 mutant. The deduced amino acid sequence shared an identity of 73% with the LYS2 product of Saccharomyces cerevisiae. Despite the high sequence homology of the alpha-aminoadipate reductase genes, the two yeast species differently responded to the presence of alpha-aminoadipate in the medium. Wild-type S. cerevisiae is known to be sensitive to alpha-aminoadipate, but becomes resistant when mutated to lys2. In contrast, K. lactis strains were found to be naturally resistant to alpha-aminoadipate. Therefore, the positive selection procedure for the isolation of lys2 mutants on alpha-aminoadipate, as practised in S. cerevisiae, cannot be applied to K. lactis. A possible reason of this difference may be that the catalytic rate of the alpha-aminoadipate reductase differs in the two yeasts. The EMBL/Genbank Accession No. for the KlLYS2 gene is AJ504405. |
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Keywords: | lysine LYS2 α‐aminoadipate Kluyveromyces lactis yeast |
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