@article{199401,
  keywords = {Genes, Biological Transport, Escherichia coli, Genes, Regulator, Cell Membrane, Operon, Cytoplasm, Maltose, Genetic Engineering, Galactosidases},
  author = {Silhavy and Casadaban and Shuman and Beckwith},
  title = {Conversion of beta-galactosidase to a membrane-bound state by gene fusion},
  abstract = {<p>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.</p>
},
  year = {1976},
  journal = {Proc Natl Acad Sci U S A},
  volume = {73},
  pages = {3423-7},
  month = {10/1976},
  issn = {0027-8424},
  doi = {10.1073/pnas.73.10.3423},
  language = {eng},
}