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. 1976 Oct;73(10):3423–3427. doi: 10.1073/pnas.73.10.3423

Conversion of beta-galactosidase to a membrane-bound state by gene fusion.

T J Silhavy, M J Casadaban, H A Shuman, J R Beckwith
PMCID: PMC431127  PMID: 790385

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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