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Cloning and characterization of the KlDIM1 gene from Kluyveromyces lactis encoding the m2(6)A dimethylase of the 18S rRNA.

By I Housen, Dominique Demonte, Denis Lafontaine and Jean Vandenhaute

Abstract

The KlDIM1 gene encoding the m2(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.Journal ArticleFLWINinfo:eu-repo/semantics/publishe

Topics: Biologie moléculaire, Biologie cellulaire, Acides nucléiques, synthèse des protéines, Amino Acid Sequence, Base Sequence, Cloning, Molecular, Genes, Fungal, Kluyveromyces -- enzymology -- genetics, Methyltransferases -- chemistry -- genetics, Molecular Sequence Data, Saccharomyces cerevisiae Proteins
Publisher: 'Wiley'
Year: 1997
DOI identifier: 10.1002/(SICI)1097-0061(19970630)13:8
OAI identifier: oai:dipot.ulb.ac.be:2013/110902
Provided by: DI-fusion
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