Conversion of beta-galactosidase to a membrane-bound state by gene fusion.
We have isolated a series of strains in which the lacZ gene has been fused to one of the maltose operons, such that the synthesis of beta-galactosidase (beta-D-galactoside galactohydrolase; EC 3.2.1.23) is inducible by maltose. The most frequent event that generates such fusions results in strains in which an intact lacZ gene has become a part of the malE,F operon. By using a special selection procedure, we have detected much rarer fusion events resulting in an altered beta-galactosidase molecule. In these strains, we presume that there is a hybrid protein molecule produced, comprised of an NH2-terminal amino acid sequence from a maltose transport protein (malF) and a COOH-terminal amino acid sequence from beta-galactosidase. The hybrid protein, which still retains some beta-galactosidase activity, is found in the cytoplasmic membrane. These results provide information on the component of the malF gene essential for incorporation of its product into the membrane.
D001692:Biological Transport; D002462:Cell Membrane / Q000201:enzymology*; D003593:Cytoplasm / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology* / Q000648:ultrastructure; D005696:Galactosidases / Q000378:metabolism*; D005796:Genes; D005809:Genes, Regulator; D005818:Genetic Engineering; D008320:Maltose / Q000378:metabolism; D009876:Operon
D008320:Maltose; D005696:Galactosidases