Related Experiment Video
Updated: Aug 10, 2026

Single-molecule Imaging of Gene Regulation In vivo Using Cotranslational Activation by Cleavage (CoTrAC)
Published on: March 15, 2013
Activator recruitment by the general transcription machinery: X-ray structural analysis of the Oct-1 POU domain/human
Stacy Hovde1, Craig S Hinkley, Katie Strong
1Department of Chemistry, Michigan State University, East Lansing, Michigan 48823, USA.
Abstract:
Transcriptional activation of the human U1 snRNA genes is dependent on a noncanonical octamer element contained within an upstream enhancer. The U1 octamer only weakly recruits the Oct-1 POU domain, although recruitment is stimulated by a peptide containing the Oct-1-binding domain of SNAP190. Structural analysis of the Oct-1 POU domain/U1 octamer/SNAP190 peptide complex revealed that SNAP190 makes extensive protein contacts with the Oct-1 POU-specific domain and with the DNA phosphate backbone within the enhancer. Although SNAP190 and OCA-B both interact with the Oct-1 POU domain through the same Oct-1 interface, a single nucleotide within the U1 octamer ablates OCA-B recruitment without compromising activator recruitment by SNAP190.
Related Concept Videos
RNA Polymerase II Accessory Proteins
Co-activators and Co-repressors
Eukaryotic Transcription Activators
The binding domains are capable of recognizing and interacting with regulatory sequences on the DNA. These domains are...
General Transcription Factors
RNA Polymerase II Accessory Proteins
Co-activators and Co-repressors

