Related Experiment Video
Updated: Oct 14, 2025

DNA-affinity-purified Chip DAP-chip Method to Determine Gene Targets for Bacterial Two component Regulatory Systems
Published on: July 21, 2014
Structural insight into DNA recognition by bacterial transcriptional regulators of the SorC/DeoR family
Markéta Šoltysová1, Irena Sieglová1, Milan Fábry2
1Structural Biology, Institute of Organic Chemistry and Biochemistry of Czech Academy of Sciences, Flemingovo nám. 2, 166 10 Prague, Czech Republic.
Abstract:
The SorC/DeoR family is a large family of bacterial transcription regulators that are involved in the control of carbohydrate metabolism and quorum sensing. To understand the structural basis of DNA recognition, structural studies of two functionally characterized SorC/DeoR family members from Bacillus subtilis were performed: the deoxyribonucleoside regulator bsDeoR and the central glycolytic genes regulator bsCggR. Each selected protein represents one of the subgroups that are recognized within the family. Crystal structures were determined of the N-terminal DNA-binding domains of bsDeoR and bsCggR in complex with DNA duplexes representing the minimal operator sequence at resolutions of 2.3 and 2.1 Å, respectively. While bsDeoRDBD contains a homeodomain-like HTH-type domain, bsCggRDBD contains a winged helix-turn-helix-type motif. Both proteins form C2-symmetric dimers that recognize two consecutive major grooves, and the protein-DNA interactions have been analyzed in detail. The crystal structures were used to model the interactions of the proteins with the full DNA operators, and a common mode of DNA recognition is proposed that is most likely to be shared by other members of the SorC/DeoR family.
Related Concept Videos
Cooperative Binding of Transcription Regulators
Cis-regulatory Sequences
Co-activators and Co-repressors
Prokaryotic Transcriptional Activators and Repressors
Transcription of prokaryotic...
Operons
RNA Polymerase II Accessory Proteins

