Title |
Characterization of components of a reducing system for SoxR in the cytoplasmic membrane of Escherichia coli |
Author |
Kang-Lok Lee1*, Kyung-Chang Lee2, Joon-Hee Lee3, and Jung-Hye Roe2 |
Address |
1Department of Biology Education, IALS, Gyeongsang National University, Jinju 52828, Republic of Korea, 2Laboratory of Molecular Microbiology, School of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 08826, Republic of Korea, 3College of Pharmacy, Pusan National University, Pusan 46241, Republic of Korea |
Bibliography |
Journal of Microbiology, 60(4),387-394, 2022,
|
DOI |
10.1007/s12275-022-1667-1
|
Key Words |
Fe-S, NADH, RseC, ApbE, Rsx, Rnf |
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. |