Repression of deoP2 in Escherichia coli by CytR: conversion of a transcription activator into a repressor

In the deoP2 promoter of Escherichia coli, a transcription activator, cAMP- CRP, binds at two sites, centered at -41.5 and -93.5 from the start site of transcription, while a repressor, CytR, binds to a space between the two c AMP-CRP complexes. The mechanisms for the cAMP-CRP-mediated transcription a ctivation and CytR-mediated transcription repression were investigated in v itro using purified components. We classified the deoP2 promoter as a class II cAMP-CRP-dependent promoter, primarily by the action of cAMP-CRP at the downstream site. Interestingly, we also found that deoP2 carries an 'UP-el ement' immediately upstream of the downstream cAMP-CRP site. The UP-element overlaps with the DNA site for CytR. However, it was observed that CytR fu nctions with the RNA polymerase devoid of the C-terminal domain of the (x-s ubunit as well as with intact RNA polymerase. The mechanism of repression b y CytR proposed in this study is that the cAMP-CRP bound at -41.5 undergoes an allosteric change upon direct interaction with CytR such that it no lon ger maintains a productive interaction with the N-terminal domain of a, but instead acts as a repressor to interfere with RNA polymerase acting on deo P2.