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Cloning and Characterization of the KlDIM1 Gene from Kluyveromyces lactis Encoding the m 2 6 A Dimethylase of the 18S rRNA
Author(s) -
HOUSEN ISABELLE,
DEMONTÉ DOMINIQUE,
LAFONTAINE DENIS,
VANDENHAUTE JEAN
Publication year - 1997
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/(sici)1097-0061(19970630)13:8<777::aid-yea140>3.0.co;2-1
Subject(s) - biology , kluyveromyces lactis , complementation , gene , genetics , saccharomyces cerevisiae , cloning (programming) , amplicon , escherichia coli , protein fragment complementation assay , mutant , ribosomal rna , microbiology and biotechnology , polymerase chain reaction , computer science , programming language
The KlDIM1 gene encoding the m 2 6 A rRNA dimethylase was cloned from a Kluyveromyces lactis genomic library using a PCR amplicon from the Saccharomyces cerevisiae ScDIM1 gene as probe. The KlDIM1 gene encodes a 320‐amino acid protein which shows 81% identity to ScDim1p from S. cerevisiae and 25% identity to ksgAp from Escherichia coli . Complementation of the kasugamycin‐resistant ksgA ‐mutant of E. coli lacking dimethylase activity demonstrates that KlDim1p is the functional homologue of the bacterial enzyme. Multiple alignment of dimethylases from prokaryotes and yeasts shows that the two yeast enzymes display distinctive structural motives including a putative nuclear localization signal. © 1997 John Wiley & Sons, Ltd.