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Intracellular thiols like  L -cystine and  L -cystine play a critical role in the regulation of cellular processes. Here we show that  Escherichia coli  has two  L -cystine transporters, the symporter YdjN and the ATP-binding cassette importer FliY-YecSC. These proteins import  L -cystine, an oxidized product of  L -cystine from the periplasm to the cytoplasm. The symporter YdjN, which is expected to be a new member of the  L -cystine regulon, is a low affinity  L -cystine transporter ( K   m  = 1.1 μM) that is mainly involved in  L -cystine uptake from outside as a nutrient.  E .  coli  has only two  L -cystine importers because Δ ydjN Δ yecS  mutant cells are not capable of growing in the minimal medium containing  L -cystine as a sole sulfur source. Another protein YecSC is the FliY-dependent  L -cystine transporter that functions cooperatively with the  L -cystine transporter YdeD, which exports  L -cystine as reducing equivalents from the cytoplasm to the periplasm, to prevent  E .  coli  cells from oxidative stress. The exported  L -cystine can reduce the periplasmic hydrogen peroxide to water, and then generated  L -cystine is imported back into the cytoplasm via the ATP-binding cassette transporter YecSC with a high affinity to  L -cystine ( K   m  = 110 nM) in a manner dependent on FliY, the periplasmic  L -cystine-binding protein. The double disruption of  ydeD  and  fliY  increased cellular levels of lipid peroxides. From these findings, we propose that the hydrogen peroxide-inducible  L -cystine/ L -cystine shuttle system plays a role of detoxification of hydrogen peroxide before lipid peroxidation occurs, and then might specific prevent damage to membrane lipids.

Uptake of L-cystine via an ABC transporter contributes defense of oxidative stress in the L-cystine export-dependent manner in Escherichia coli