Open AccessAnalysis of a eukaryotic β-galactostdase gene: the N-terminal end of the yeastKluyveromyces lactisprotein shows homology to theEscherichia coli lacZgene product
Author(s) -
Karin D. Breunig,
Ulrike Dahlems,
Sunil Das,
Cornelis P. Hollenberg
Publication year - 1984
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/12.5.2327
Subject(s) - kluyveromyces lactis , biology , gene , homology (biology) , kluyveromyces , saccharomyces cerevisiae , escherichia coli , peptide sequence , lac operon , coding region , nucleic acid sequence , microbiology and biotechnology , genetics
The LAC4 gene of Kluyveromyces lactis, encoding the enzyme beta-galactosidase was mapped on a cloned DNA fragment and the sequence of the 5' end was determined. This sequence includes the 5' regulatory region involved in the induction by lactose and the N-terminal end of the protein coding region. Comparison of the deduced amino acid sequence of this eukaryotic enzyme with the N-terminal end of the Escherichia coli beta-galactosidase revealed substantial homology. Two major RNA initiation sites were mapped at -115 and -105. A number of structural peculiarities of the 5'non-coding region are discussed as in comparison to Saccharomyces cerevisiae genes.