Mutant of Escherichia coli Exhibiting a Cold-sensitive Phenotype for Growth on Lactose
Author(s) -
Catherine K. Squires,
John L. Ingraham
Publication year - 1969
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.97.2.488-494.1969
Subject(s) - galactokinase , galactose , lactose , mutant , biology , biochemistry , escherichia coli , beta galactosidase , transferase , gal operon , uridine diphosphate , operon , lac operon , enzyme , gene
As part of a study on the effect of low temperature on cellular regulatory processes, a class of lactose-negative mutants ofEscherichia coli K-12 was isolated which could use lactose as a sole carbon and energy source at 37 C, but which could not use this sugar at 20 C. The lactose operon of the mutants functioned normally at 20 C. Galactose exhibited a strong inhibitory effect on growth, especially at 20 C. Growth of the mutants on glycerol was stopped at 20 C and slowed considerably at 37 C if galactose was added to the medium. Making the mutants galactose-positive eliminated the cold sensitivity of lactose utilization. One mutant was shown to be galactose-1-phosphate uridyl transferase-negative, galactose-kinase heat-sensitive, and uridine diphosphate-galactose-4-epimerase-positive. It is postulated that the mutant is able to phosphorylate galactose at 20 C (if only at a very low rate), but lacking transferase it is poisoned by the accumulation of galactose-1-phosphate. At 37 C, galactokinase is nonfunctional and the mutant grows on the glucose moiety of lactose.
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