Related Experiment Video
Updated: Jul 4, 2026

Single-molecule Imaging of Gene Regulation In vivo Using Cotranslational Activation by Cleavage (CoTrAC)
Published on: March 15, 2013
Identification of the subunit of cAMP receptor protein (CRP) that functionally interacts with CytR in
K L Meibom1, B H Kallipolitis, R H Ebright
1Department of Molecular Biology, Odense University Campusvej 55, DK-5230 Odense M, Denmark. molbiol@molbiol.sdu.dk
Abstract:
At promoters of the Escherichia coli CytR regulon, the cAMP receptor protein (CRP) interacts with the repressor CytR to form transcriptionally inactive CRP-CytR-promoter or (CRP)(2)-CytR-promoter complexes. Here, using "oriented heterodimer" analysis, we show that only one subunit of the CRP dimer, the subunit proximal to CytR, functionally interacts with CytR in CRP-CytR-promoter and (CRP)(2)-CytR-promoter complexes. Our results provide information about the architecture of CRP-CytR-promoter and (CRP)(2)-CytR-promoter complexes and rule out the proposal that masking of activating region 2 of CRP is responsible for the transcriptional inactivity of the complexes.
Related Concept Videos
RNA Polymerase II Accessory Proteins
Cis-regulatory Sequences
Prokaryotic Transcriptional Activators and Repressors
Transcription of prokaryotic...
Co-activators and Co-repressors
Repressible Operon: trp Operon
Global Regulatory Systems

