Yeast genes fused to beta-galactosidase in Escherichia coli can be expressed normally in yeast.

AUTOR(ES)

Rose, M

RESUMO

A plasmid was constructed that allows the selection in vivo of gene fusions between the Escherichia coli beta-galactosidase gene and the yeast (Saccharomyces cerevisiae) URA3 gene. A large yeast DNA fragment containing the URA3 gene was placed upstream of an amino-terminally deleted version of the lacZ gene. The plasmid vehicle contains sequences that allow selection and maintenance of the plasmid in both yeast and E. coli. Selection for Lac+ in E. coli yielded numerous deletions that fused the lacZ gene to the URA3 gene and flanking yeast sequences, to the bacterial tetracycline-resistance gene from the parent plasmid pBR322, and to the yeast 2-micrometer plasmid DNA. Some of these fusion plasmids produced beta-galactosidase activity when introduced into yeast. One of the fusions to the URA3 gene itself has been shown to place the expression of beta-galactosidase activity under uracil regulation in yeasts.

Documentos Relacionados

• Efflux of beta-galactosidase products from Escherichia coli.
• Genetic studies on the inability of beta-galactosidase to be translocated across the Escherichia coli cytoplasmic membrane.
• 72 residues of gal repressor fused to beta-galactosidase repress the gal operon of E. coli.
• Kinectics of beta-galactosidase synthesis in Escherichia coli at 5 C.
• The amino acid sequence of beta-galactosidase of Escherichia coli.