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Title: Cu Transport by the Extended Family of CcoA-like Transporters (CalT) in Proteobacteria

Journal Article · · Scientific Reports
 [1];  [2];  [3];  [4];  [5]; ORCiD logo [6];  [3];  [7]
  1. Univ. of Pennsylvania, Philadelphia, PA (United States); Xiamen Univ., Xiamen (China)
  2. Brookhaven National Lab. (BNL), Upton, NY (United States)
  3. Univ. of Pennsylvania, Philadelphia, PA (United States)
  4. Univ. of Pennsylvania, Philadelphia, PA (United States); Geisel School of Medicine at Dartmouth, Hanover, NH (United States)
  5. Univ. of Chile, Santiago (Chile)
  6. Albert-Ludwigs-Univ.Freiburg, Freiburg (Germany)
  7. Univ. of Pennsylvania, Philadelphia, PA (United States); UMR CNRS 5254 and Univ. de Pau et des Pays de l'Adour, Pau (France)

Comparative genomic studies of the bacterial MFS-type copper importer CcoA, required for cbb3-type cytochrome c oxidase (cbb3-Cox) biogenesis, revealed a widespread CcoA-like transporters (CalT) family, containing the conserved CcoA Cu-binding MxxxM and HxxxM motifs. Surprisingly, this family also included the RfnT-like proteins, earlier suggested to transport riboflavin. However, presence of the Cu-binding motifs in these proteins raised the possibility that they might be Cu transporters. To test this hypothesis, the genomic context of the corresponding genes was examined, and three of such genes from Ochrobactrum anthropi, Rhodopseudomonas palustris and Agrobacterium tumefaciens were expressed in Escherichia coli (ΔribB) and Rhodobacter capsulatus (ΔccoA) mutants. Copper and riboflavin uptake abilities of these strains were compared with those expressing R. capsulatus CcoA and Rhizobium leguminosarum RibN as bona fide copper and riboflavin importers, respectively. Altogether data demonstrated that the “RfnT-like” CalT proteins are unable to efficiently transport riboflavin, but they import copper like CcoA. Nevertheless, even though expressed and membrane-localized in a R. capsulatus mutant lacking CcoA, these transporters were unable to accumulate Cu or complement for cbb3-Cox defect. This lack of functional exchangeability between the different subfamilies of CalT homologs suggests that MFS-type bacterial copper importers might be species-specific.

Research Organization:
Univ. of Pennsylvania, Philadelphia, PA (United States); Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences, and Biosciences Division; USDOE Office of Science (SC), Biological and Environmental Research (BER)
Grant/Contract Number:
FG02-91ER20052; SC0012704
OSTI ID:
1497377
Alternate ID(s):
OSTI ID: 1597464
Report Number(s):
BNL-211298-2019-JAAM
Journal Information:
Scientific Reports, Vol. 9, Issue 1; ISSN 2045-2322
Publisher:
Nature Publishing GroupCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 7 works
Citation information provided by
Web of Science

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Cited By (1)

The cbb 3 -type cytochrome oxidase assembly factor CcoG is a widely distributed cupric reductase journal September 2019