Methyl galactosidase activity: an alternative evolutionary destination for the ebgA0 gene

Author:

Hall B G

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference5 articles.

1. Evolution of a second gene for f-galactosidase in Escherichia coli;Campbell J. H.;Proc. Natl. Acad. Sci. U.S.A.,1973

2. Regulation of newly evolved enzymes. I. Selection of a novel lactase regulated by lactose in Escherichia coli;Hall B. G.;Genetics,1974

3. Regulation of newly evolved enzymes. II. The ebg repressor;Hall B. G.;Genetics,1975

4. A second naturally occurring fi-galactosidase inE. coli;Hart I;Nature (London),1974

5. Miller J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Cold Spring Harbor N.Y.

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