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      Microorganisms as Model Systems for Studying Evolution 

      The Evolved β-Galactosidase System of Escherichia coli

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      Springer US

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          A quantitation of the factors which affect the hydrolase and transgalactosylase activities of β-galactosidase (E. coli) on lactose

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            lac repressor-operator interaction

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              Evolution of a new enzymatic function by recombination within a gene.

              Mutations that alter the ebgA gene so that the evolved beta-galactosidase (ebg) enzyme of Escherichia coli can hydrolyze lactose fall into two classes: class I mutants use only lactose, whereas class II mutants use lactulose as well as lactose. Neither class uses galactosylarabinose effectively. In this paper we show that when both a class I and a class II mutation are present in the same ebgA gene, ebg enzyme acquires a specificity for galactosylarabinose. Although galactosylarbinose utilization can evolve as the consequence of sequential spontaneous mutations, it can also evolve via intragenic recombination in crosses between class I and class II ebgA+ mutant strains. We show that the sites for class I and class II mutations lie about 1 kilobase, or about a third of the gene, apart in ebgA. Implications of these findings with respect to the evolution of new metabolic functions discussed.
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                Author and book information

                Book Chapter
                1984
                : 165-185
                10.1007/978-1-4684-4844-3_6
                8f58971c-26b6-4620-bff3-d43ead2e0356
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