PMID:790385

Citation	Silhavy, TJ, Casadaban, MJ, Shuman, HA and Beckwith, JR (1976) Conversion of beta-galactosidase to a membrane-bound state by gene fusion. Proc. Natl. Acad. Sci. U.S.A. 73:3423-7
Abstract	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.
Links	PubMed PMC431127
Keywords	Biological Transport; Cell Membrane/enzymology; Cytoplasm/enzymology; Escherichia coli/enzymology; Escherichia coli/ultrastructure; Galactosidases/metabolism; Genes; Genes, Regulator; Genetic Engineering; Maltose/metabolism; Operon
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