Abstract
A reducing system of SoxR, a regulator of redox-active molecules,
was identified as rsxABCDGE gene products and RseC
in Escherichia coli through genetic studies. We found that
ApbE was an additional component of the reducer system.
Bacterial two hybrid analysis revealed that these proteins indeed
had multiple interactions among themselves. RseC and
RsxB formed the core of the complex, interacting with more
than five other components. RsxC, the only cytoplasmic component
of the system, interacted with SoxR. It might be linked
with the rest of the complex via RsxB. Membrane fractions
containing the wild type complex but not the mutant complex
reduced purified SoxR using NADH as an electron source.
These results suggest that Rsx genes, RseC, and ApbE can
form a complex using NAD(P)H to reduce SoxR.
Citations
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