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Table 1 VieB specifically interacts with VieS-C

From: The VieB auxiliary protein negatively regulates the VieSA signal transduction system in Vibrio cholerae

Protein Combination Native Oligomeric State Hetero-association stoichiometry K D (μM)
VieS-C + VieA-His6 VieS-C VieA-His 6 1 dimer : 1 dimer 1.38 ± 0.35
Dimer (MW = 150 kDa) Dimer (MW = 130 KDa)
VieS-C + VieB VieS-C VieB 1 dimer : 1 monomer 0.467 ± 0.054
Dimer (MW = 150 kDa) Monomer (MW = 64 kDa)
VieS-C + VieB D62E VieS-C VieB D62E 1 dimer : 1 monomer 0.197 ± 0.061
Dimer (MW = 150 kDa) Monomer (MW = 64 kDa)
VieA-His6 + VieB VieA-His 6 VieB N/A N/A
Dimer (MW = 130 kDa) Monomer (MW = 64 kDa)
  1. Characterization of VieS-C, VieA-His6, wild-type VieB and the VieB D62E point mutant (self-association) were determined by Size-Exclusion Chromatography Multi-angle Light Scattering. To determine the protein-protein interactions of various VieSAB protein combinations, hetero-association interaction kinetics were determined over a range of protein concentrations by Composition-gradient Multi-angle Light Scattering. Data for the hetero-association stoichiometry are represented in monomer units. These data represent the average and ± SD of three independently purified replicates.