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Title: The Cu chaperone CopZ is required for Cu homeostasis in Rhodobacter capsulatus and influences cytochrome cbb3 oxidase assembly

Journal Article · · Molecular Microbiology
DOI:https://doi.org/10.1111/mmi.14190· OSTI ID:1597471
 [1];  [1];  [1];  [2];  [1];  [3]; ORCiD logo [1]
  1. Albert-Ludwigs-Universität Freiburg (Germany)
  2. Albert-Ludwigs-Universität Freiburg (Germany); Univ. of Pennsylvania, Philadelphia, PA (United States)
  3. Univ. of Pennsylvania, Philadelphia, PA (United States)

We present that Cu homeostasis depends on a tightly regulated network of proteins that transport or sequester Cu, preventing the accumulation of this toxic metal while sustaining Cu supply for cuproproteins. In Rhodobacter capsulatus, Cu-detoxification and Cu delivery for cytochrome c oxidase (cbb3-Cox) assembly depend on two distinct Cu-exporting P1B-type ATPases. The low-affinity CopA is suggested to export excess Cu and the high-affinity CcoI feeds Cu into a periplasmic Cu relay system required for cbb3-Cox biogenesis. In most organisms, CopA-like ATPases receive Cu for export from small Cu chaperones like CopZ. However, whether these chaperones are also involved in Cu export via CcoI-like ATPases is unknown. Here we identified a CopZ-like chaperone in R. capsulatus, determined its cellular concentration and its Cu binding activity. Our data demonstrate that CopZ has a strong propensity to form redox-sensitive dimers via two conserved cysteine residues. A ΔcopZ strain, like a ΔcopA strain, is Cu-sensitive and accumulates intracellular Cu. In the absence of CopZ, cbb3-Cox activity is reduced, suggesting that CopZ not only supplies Cu to P1B-type ATPases for detoxification but also for cuproprotein assembly via CcoI. In conclusion, this finding was further supported by the identification of a ~150 kDa CcoI-CopZ protein complex in native R. capsulatus membranes.

Research Organization:
Univ. of Pennsylvania, Philadelphia, PA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES); German Research Foundation (DFG); National Institutes of Health (NIH)
Grant/Contract Number:
FG02-91ER20052; GRK2202; IRTG1478; GM38237
OSTI ID:
1597471
Alternate ID(s):
OSTI ID: 1493074
Journal Information:
Molecular Microbiology, Vol. 111, Issue 3; ISSN 0950-382X
Publisher:
WileyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 16 works
Citation information provided by
Web of Science

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  • M., Stothard, P. ; Rouani, M. ; Sundararaj, S. ; Wishart, D. S. ; Nazhad, B. H. ; Guo, A. ; Ellison,
  • University of Alberta Libraries https://doi.org/10.7939/r3kd1qw7c
text January 2004

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