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The copper supply pathway to a S almonella C u, Z n‐superoxide dismutase ( SodCII ) involves P 1 B ‐type ATPase copper efflux and periplasmic CueP
Author(s) -
Osman Deenah,
Patterson Carl J.,
Bailey Kathryn,
Fisher Karl,
Robinson Nigel J.,
Rigby Stephen E. J.,
Cavet Jennifer S.
Publication year - 2013
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12107
Subject(s) - periplasmic space , biology , biochemistry , superoxide dismutase , virulence , microbiology and biotechnology , mutant , salmonella enterica , copper , escherichia coli , enzyme , chemistry , gene , organic chemistry
Summary Periplasmic Cu , Zn ‐superoxide dismutases ( Cu , Zn ‐ SODs ) are implicated in bacterial virulence. It has been proposed that some bacterial P 1 B ‐type ATPases supply copper to periplasmic cupro‐proteins and such transporters have also been implicated in virulence. Here we show that either of two P 1 B ‐type ATPases , CopA or GolT , is needed to activate a periplasmic C u, Z n‐ SOD ( SodCII ) in S almonella enterica serovar Typhimurium. A Δ copA /Δ golT mutant accumulates inactive Zn ‐ SodCII which can be activated by copper‐supplementation in vitro . In contrast, either single ATPase mutant accumulates fully active Cu , Zn ‐ SodCII . A contribution of GolT to copper handling is consistent with its copper‐responsive transcription mediated by DNA ‐binding metal‐responsive activator GolS . The requirement for duplicate transcriptional activators CueR and GolS remains unclear since both have similar tight K Cu . Mutants lacking periplasmic cupro‐protein CueP also accumulate inactive Z n‐ SodCII and while CopA and GolT show functional redundancy, both require CueP to activate SodCII in vivo . Zn ‐ SodCII is also activated in vitro by incubation with Cu ‐ CueP and this coincides with copper transfer as monitored by electron paramagnetic resonance spectroscopy. These experiments establish a role for CueP within the copper supply pathway for S almonella Cu , Zn ‐ SodCII . Copper binding by CueP in this pathogen may confer protection of the periplasm from copper‐mediated damage while sustaining vital cupro‐enzyme activity.