Mechanism underlying autoinducer recognition in the Vibrio cholerae DPO-VqmA quorum-sensing pathway
Xiuliang Huang, Olivia P. Duddy, Justin E. Silpe, Jon E. Paczkowski, Jian-Ping Cong, Brad R. Henke, Bonnie L. Bassler
Abstract
-alanyl-aminoacetone (Ala-AA), also bound and activated VqmA. Results from site-directed mutagenesis and competitive ligand-binding analyses revealed that DPO and Ala-AA occupy the same binding site. In summary, our structure-function analysis identifies key features required for VqmA activation and DNA binding and establishes that, whereas VqmA binds two different ligands, VqmA does not require a bound ligand for folding or basal transcriptional activity. However, bound ligand is required for maximal activity.
Topics & Concepts
AutoinducerQuorum sensingVibrio choleraeChemistryTranscription factorBinding siteTranscription (linguistics)Conformational changeCell biologyLigand (biochemistry)MutantBiochemistryBiologyGeneBacteriaReceptorGeneticsVirulenceLinguisticsPhilosophyVibrio bacteria research studiesBacterial biofilms and quorum sensingBacterial Genetics and Biotechnology