Abstract
Previous studies (Campbell et al., 1973; Hall and Hartl, 1974; Hall and Hartl, 1975) have shown that the ebgA0 gene, whose product does not hydrolyze lactose may evolve so that its product does hydrolyze lactose; i.e., lactase activity is one evolutionary destination of the ebgA0 gene. Beginning with a strain that synthesizes ebgA0 gene product constitutively and grows extremely slowly (doubling time, 30 to 50 h) on methyl-beta-D-galactopyranoside (MG), a derivative was selected capable of growth on MG at a moderate rate (doubling time, 5.9 h). Genetic evidence is presented showing that the gene that permits growth on MG is an allele of ebgA. A comparison among strains bearing several alleles of ebgA shows that the new allele, termed ebgAmg, synthesizes a product specific for MG and thus represents a true alternative evolutionary destination for the ebgA0 gene.
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Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Campbell J. H., Lengyel J. A., Langridge J. Evolution of a second gene for beta-galactosidase in Escherichia coli. Proc Natl Acad Sci U S A. 1973 Jun;70(6):1841–1845. doi: 10.1073/pnas.70.6.1841. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gall B. G., Hartl D. L. Regulation of newly evolved enzymes. II. The ebg repressor. Genetics. 1975 Nov;81(3):427–435. doi: 10.1093/genetics/81.3.427. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hall B. G., Hartl D. L. Regulation of newly evolved enzymes. I. Selection of a novel lactase regulated by lactose in Escherichia coli. Genetics. 1974 Mar;76(3):391–400. doi: 10.1093/genetics/76.3.391. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hartl D. L., Hall B. G. Second naturally occurring beta-galactosidase in E. coli. Nature. 1974 Mar 8;248(5444):152–153. doi: 10.1038/248152a0. [DOI] [PubMed] [Google Scholar]
