title: Snap denaturation reveals dimerization by AraC-like protein Rns.
abstract: Here we show that the Rns regulator of Escherichia coli dimerises in vivo and in vitro. Furthermore, we demonstrate that Rns forms aggregates in vitro and describe a methodology to ameliorate aggregation thus permitting the analysis of Rns by cross-linking.
authors.affiliation: Department of Clinical Microbiology, School of Medicine, Trinity College Dublin, St. James's Hospital, Dublin, Ireland.
authors.forename: Vivienne
authors.initials: V
authors.lastname: Mahon
authors.forename: Robert P
authors.initials: RP
authors.lastname: Fagan
authors.forename: Stephen G J
authors.initials: SG
authors.lastname: Smith
mesh_terms: D051777:AraC Transcription Factor / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D011489:Protein Denaturation; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D015534:Trans-Activators / Q000737:chemistry* / Q000378:metabolism
chemical_list: D051777:AraC Transcription Factor; C497371:AraC protein, E coli; D029968:Escherichia coli Proteins; D011993:Recombinant Fusion Proteins; C108303:Rns protein, bacteria; D015534:Trans-Activators