GAL2 codes for a membrane-bound subunit of the galactose permease in Saccharomyces cerevisiae
Open Access
- 1 April 1986
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 166 (1) , 313-318
- https://doi.org/10.1128/jb.166.1.313-318.1986
Abstract
The gene encoding the galactose permease of Saccharomyces cerevisiae (GAL2) was cloned. The clone restores galactose permease activity to gal2 yeasts and is regulated by galactose in a manner similar to other GAL gene products (GAL1, -7, and -10). Experiments with temperature-conditional secretory mutants indicated that transport of the GAL2 gene product to the cell surface requires a functional secretory pathway. In addition, gene fusions were constructed between the GAL2 gene and the Escherichia coli lacZ gene. The GAL2-lacZ gene fusions code for galactose-regulated beta-galactosidase activity in yeasts. The beta-galactosidase activity was found to be membrane bound.This publication has 30 references indexed in Scilit:
- Intracellular targeting and import of an F1-ATPase beta-subunit-beta-galactosidase hybrid protein into yeast mitochondria.Proceedings of the National Academy of Sciences, 1984
- Targeting of E. coli β-galactosidase to the nucleus in yeastCell, 1984
- Yeast secretory mutants that block the formation of active cell surface enzymes.The Journal of cell biology, 1984
- Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuoleCell, 1982
- The organization and transcription of the galactose gene cluster of SaccharomycesJournal of Molecular Biology, 1981
- Order of events in the yeast secretory pathwayCell, 1981
- Compartmentalized assembly of oligosaccharides on exported glycoproteins in yeastCell, 1981
- Identification of 23 complementation groups required for post-translational events in the yeast secretory pathwayCell, 1980
- The structure of transposable yeast mating type lociCell, 1980
- Transformation of yeast by a replicating hybrid plasmidNature, 1978