Q.In E. coli, the lac operon gets switched on when:
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Start your 14-day free trial to unlock the full solution →The lac operon in E. coli switches on when lactose is present and binds to the repressor protein, preventing the repressor from blocking transcription.
The lac operon is a classic example of gene regulation in prokaryotes, specifically in the bacterium Escherichia coli. Its primary function is to allow E. coli to efficiently metabolize lactose only when glucose, its preferred energy source, is unavailable. This system ensures that the cell doesn't waste energy producing enzymes for lactose metabolism if lactose isn't present or if a better sugar (glucose) is at hand.
At its core, the lac operon consists of several key genetic components:
- A regulator gene (i gene): This gene is located upstream of the operon and constitutively produces a repressor protein.
- A promoter (p): This is the binding site for RNA polymerase, the enzyme responsible for initiating transcription.
- An operator (o): Situated between the promoter and the structural genes, this is the binding site for the repressor protein.
- Structural genes: These include lacZ, lacY, and lacA.
- lacZ codes for $\beta$-galactosidase, which hydrolyzes lactose into glucose and galactose.
- lacY codes for permease, which increases the cell's permeability to lactose, allowing it to enter the cell.
- lacA codes for transacetylase, whose exact role in lactose metabolism is not fully understood but is part of the operon.
When lactose is absent from the environment, the lac operon remains switched off. The regulator (i) gene continuously synthesizes the repressor protein. This repressor protein is active and readily binds to the operator region of the operon. When the repressor is bound to the operator, it physically blocks RNA polymerase from moving along the DNA and transcribing the structural genes. Consequently, no enzymes for lactose metabolism are produced, conserving the cell's resources.
The repressor protein has a high affinity for the operator sequence, ensuring that in the absence of lactose, the operon is effectively shut down.
The situation changes dramatically when lactose becomes available. Lactose, or more precisely, its isomer allolactose (which is formed in small amounts from lactose by $\beta$-galactosidase), acts as an inducer. When allolactose is present, it binds to the repressor protein. This binding causes a conformational change in the repressor protein, altering its shape.
The binding of allolactose to the repressor is crucial. It's this interaction that inactivates the repressor.
Once the repressor protein's conformation changes, it can no longer bind to the operator region. With the operator site now free, RNA polymerase can bind to the promoter and proceed to transcribe the structural genes (lacZ, lacY, lacA). This leads to the production of $\beta$-galactosidase, permease, and transacetylase, enabling the E. coli cell to take up and metabolize lactose. This entire process, where the presence of a substrate (lactose) leads to the expression of genes required for its metabolism, is known as induction. …
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