Related Experiment Video
Updated: Jul 22, 2026

Application of an In vitro DNA Protection Assay to Visualize Stress Mediation Properties of the Dps Protein
Published on: May 31, 2013
The interaction of the ferric uptake regulation protein with DNA
1Chemical Biodynamics, University of California, Berkeley 94720, USA.
Abstract:
The interaction of the Ferric Uptake Regulation (Fur) protein with the backbone of operator DNA was analyzed by hydroxyl radical footprinting and the ethylation interference assay. Comparison of the contacts made by Fur and those made by proteins containing the helix-turn-helix or related motifs shows that the mode of DNA binding by this repressor is unique. Ethylation interference experiments demonstrate that there are relatively few phosphate contacts of unique disposition while hydroxyl radical footprinting demonstrates that Fur-operator contacts are segregated on one face of the helix and span nearly three successive major grooves.
More Related Videos
Related Concept Videos
RNA Polymerase II Accessory Proteins
Cooperative Binding of Transcription Regulators
Co-activators and Co-repressors
Eukaryotic Transcription Inhibitors
Eukaryotic transcription inhibitors usually contain two distinct domains, a DNA...
The Early Endosome: Endocytosis of Transferrin
Transcriptional Regulation: Riboswitches

