The cytoplasmic Cu+‐chaperones of Pseudomonas aeruginosa

• DOI: 10.1096/fasebj.2018.32.1_supplement.803.4
• Publication Date: 2021-06-21T16:34:04Z
• Authors: Lorena Novoa‐Aponte; Jose M. Arguello
• Keywords: Chaperone (clinical); Efflux

Copper is a micronutrient required by multiple enzymes as redox co‐factor. However, free Cu toxic, leading to Fe‐S cluster disassembly and reactive oxygen species. As such, immune cells use phagosomal Cu‐overload clear pathogens. Thus, bacteria need direct correct targets while maintaining non‐toxic levels. To limit toxicity, sequester drive the efflux of using various mechanisms. Among these, single cytoplasmic Cu‐chaperones mobilize metal within cell compartments. We recently used RNA‐seq show that Pseudomonas has network proteins among cellular Importantly, our study uncovered unusual presence two putative in these (CopZ1 CopZ2). Both are under control Cu‐sensor CueR consequently copZ1 copZ2 expression induced exposure Cu. Why there ? why do both respond Cu‐imbalances? hypothesize metabolically linked via Cu‐exchange, deliver different targets. have observed CopZ1 CopZ2 share 37% identity (51% similarity), contain invariant Cu‐binding motif (CxxC), exhibit similar secondary structure line with βαββαβ‐fold, characteristic Cu‐chaperones. bind 1:1 stoichiometry sub‐femtoMolar affinities. 100‐times higher affinity for compared CopZ1. determined exchange between proteins. expected from constants, Cu‐exchange equilibrium displaced formation metallated‐CopZ2 form. Interestingly, chaperones able transfer non‐cognate other organisms, suggesting limited molecular recognition during metal‐exchange. Although genes equally Cu‐stress, we 10‐times more abundant than CopZ1, resting conditions upon stress. The differential response (affinities), protein levels, their distinct electrostatic surface potential suggest perhaps receive molecules. Currently, testing which Cu‐donors. Support or Funding Information This work was supported NIH Grant R01 GM114949 J.M.A.. abstract Experimental Biology 2018 Meeting. There no full text article associated this published FASEB Journal .