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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1973 Jun;70(6):1841–1845. doi: 10.1073/pnas.70.6.1841

Evolution of a Second Gene for β-Galactosidase in Escherichia coli

John H Campbell *, Judith A Lengyel , John Langridge
PMCID: PMC433609  PMID: 4124306

Abstract

Mutants of E. coli K12 with deletions of the β-galactosidase gene (lacZ) can reacquire the ability to hydrolyze β-galactosides during prolonged intense selection for growth on lactose. Full lactose competence is restored through a sequence of at least five mutations. Cell extracts of these derived strains hydrolyze o-nitrophenyl-β-D-galactoside, the standard substrate for assay of β-galactosidase. The enzyme responsible for this activity differs in its immunological, kinetic, and sedimentation characteristics from the lacZ β-galactosidase of wild-type E. coli. Its genetic determinant, designated ebg-5, maps at 59 min on the E. coli chromosome, whereas the lac operon maps at 10 min. We suggest that a gene not involved in lactose utilization has been progressively changed into a form capable of specifying a β-galactosidase and that this process is similar to that whereby genes with new functions are evolved by natural selection.

Keywords: lac operon, gene mapping, enzyme characterization, lactose permease, enzyme evolution

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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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