Repressors are inactivated either by interaction with a small-molecule inducer o

Question

Repressors are inactivated either by interaction with a small-molecule inducer or by proteolytic cleavage.

Repressors are inactivated either by interaction with a small-molecule inducer or by proteolytic cleavage. Why is it advantageous for a repressor like the lac repressor to be inactivated by binding to allolactose rather than by proteolytic cleavage? The inactivation of the repressor is irreversible. The inactivation of the repressor is reversible. The inactivation process allows to quickly respond to changes in medium. The inactivation process allows to gradually respond to changes in medium. The inactivation process requires resynthesis of regulatory proteins. The inactivation process does not require resynthesis of regulatory proteins.

Explanation / Answer

It is advantageous for lac repressor to be inactivated by allolactose because:

The inactivation of the repressor is reversible.

The inactivation process allows quickly to respond to changes in medium.

The inactivation process does not require resynthesis of regulatory proteins.

Lac repressor inhibits transcription of lac operon.When lactose is available, allolactose binds to lac repressor, brings a conformational change such that the repressor cannot bind with DNA. This process is reversible.

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