Manganese transporters regulate the resumption of replication in hydrogen peroxide-stressed Escherichia coli.

Following hydrogen peroxide treatment, ferrous iron (Fe) is oxidized to its ferric form (Fe), stripping it from and inactivating iron-containing proteins. Many mononuclear iron enzymes can be remetallated by manganese to restore function, while other enzymes specifically utilize manganese as a cofactor, having redundant activities that compensate for iron-depleted counterparts. DNA replication relies on one or more iron-dependent protein(s) as synthesis abates in the presence of hydrogen peroxide and requires manganese in the medium to resume.

Manganese Is Required for the Rapid Recovery of DNA Synthesis following Oxidative Challenge in .

Divalent metals such as iron and manganese play an important role in the cellular response to oxidative challenges and are required as cofactors by many enzymes. However, how these metals affect replication after oxidative challenge is not known. Here, we show that replication in is inhibited following a challenge with hydrogen peroxide and requires manganese for the rapid recovery of DNA synthesis.