Abstract:
:Periplasmic Cu,Zn-superoxide dismutases (Cu,Zn-SODs) are implicated in bacterial virulence. It has been proposed that some bacterial P(1B)-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(1B)-type ATPases, CopA or GolT, is needed to activate a periplasmic Cu,Zn-SOD (SodCII) in Salmonella enterica serovar Typhimurium. A ΔcopA/ΔgolT 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 Zn-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 Salmonella 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.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Osman D,Patterson CJ,Bailey K,Fisher K,Robinson NJ,Rigby SE,Cavet JSdoi
10.1111/mmi.12107subject
Has Abstractpub_date
2013-02-01 00:00:00pages
466-77issue
3eissn
0950-382Xissn
1365-2958journal_volume
87pub_type
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