The EBG system of E. coli: origin and evolution of a novel beta-galactosidase for the metabolism of lactose.
The EBG system of E. coli has served as a model for the evolution of novel functions. This paper reviews the experimental evolution of the catabolism of beta-galactoside sugars in strains of E. coli that carry deletions of the classical lacZ beta-galactosidase gene. Evolution of the ebgA encoded Ebg beta-galactosidase for an expanded substrate range, evolution of the ebgR encoded Ebg repressor for sensitivity to an expanded range of inducers, the amino acid replacements responsible for those changes, and the evolutionary potential of the system are discussed. The EBG system has also served as a model for studying the detailed catalytic consequences of experimental evolution at the physical-chemical level. The analysis of free-energy profiles for the wildtype and all of the various evolved Ebg enzymes has permitted rejection of the Albery-Knowles hypothesis that relates likely changes in free-energy profiles to evolutionary change.
Hall
Barry G
BG
Biology Department, Hutchinson Hall, River Campus, University of Rochester, Rochester, NY 14627-0211, USA. drbh@mail.rochester.edu
D003433:Crosses, Genetic; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism*; D029968:Escherichia coli Proteins; D019143:Evolution, Molecular; D010802:Phylogeny; D012097:Repressor Proteins / Q000235:genetics; D001616:beta-Galactosidase / Q000235:genetics*
C062847:EbgR protein, E coli; D029968:Escherichia coli Proteins; D012097:Repressor Proteins; D001616:beta-Galactosidase; C062846:evolved beta-galactosidase, E coli