The lac operon in Escherichia coli is a classic model for transcriptional regulation. The operon contains three structural genes (lacZ, lacY, lacA) controlled by a promoter and operator region. A regulatory gene, lacI, encodes the Lac repressor. When lactose is present, allolactose (an isomer of lactose) binds to the Lac repressor, causing a conformational change that prevents operator binding, allowing transcription. Additionally, when glucose is absent, elevated intracellular cAMP binds to CAP (catabolite activator protein); the cAMP–CAP complex binds to the CAP site upstream of the promoter, enhancing RNA polymerase binding and increasing transcription rate.
A research team studied a mutant strain of E. coli (strain M1) carrying a point mutation in lacI that alters the allolactose-binding site of the repressor. The mutant repressor retains full operator-binding ability but cannot bind allolactose.
β-galactosidase activity (encoded by lacZ) was measured under three conditions:
- Condition A:
2% glucose, no lactose
- Condition B:
2% lactose, no glucose
- Condition C:
1% glucose and
1% lactose
Wild-type
β-galactosidase activity was high only in Condition B. Strain M1 showed negligible
β-galactosidase activity in all three conditions.