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LYS2 gene and its mutation in Kluyveromyces lactis
Author(s) -
Alberti Adriana,
Ferrero Iliana,
Lodi Tiziana
Publication year - 2003
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.1030
Subject(s) - kluyveromyces lactis , biology , saccharomyces cerevisiae , mutant , gene , genetics , plasmid , complementation , kluyveromyces , yeast , biochemistry
The KlLYS2 gene, encoding the α‐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 α‐aminoadipate reductase genes, the two yeast species differently responded to the presence of α‐aminoadipate in the medium. Wild‐type S. cerevisiae is known to be sensitive to α‐aminoadipate, but becomes resistant when mutated to lys2 . In contrast, K. lactis strains were found to be naturally resistant to α‐aminoadipate. Therefore, the positive selection procedure for the isolation of lys2 mutants on α‐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 α‐aminoadipate reductase differs in the two yeasts. The EMBL/Genbank Accession No. for the KlLYS2 gene is AJ504405. Copyright © 2003 John Wiley & Sons, Ltd.