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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.
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BMC Microbiology

ISSN: 1471-2180

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