The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb3-type cytochrome oxidase in Rhodobacter capsulatus

Lohmeyer, Eva; Schröder, Sebastian; Pawlik, Grzegorz; Trasnea, Petru‐Iulian; Peters, Annette; Daldal, Fevzi; Koch, Hans‐Georg

doi:10.1016/j.bbabio.2012.06.621

Cited by 39 publications

(92 citation statements)

References 60 publications

(123 reference statements)

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“…Therefore, we must revise a previous interpretation according to which ScoI was not believed to be an important biogenesis factor for cytochrome cbb 3 in B. japonicum (10). Other recent studies have provided good evidence for a role of ScoI-like proteins (SenC) in cytochrome cbb 3 formation in P. aeruginosa (22), R. sphaeroides (24), and R. capsulatus (23).…”

Section: Discussionmentioning

confidence: 95%

“…Intuitively, one would like to propose that the soluble, periplasmic PcuC protein disseminates copper to the membrane-bound ScoI protein and perhaps to other membranebound recipients (e.g. CoxG/Cox11, FixI/CcoI, and CcoA), as has been suggested in part also by others (15,21,23,24). However, more biochemical work, such as establishing a copper transfer assay with purified components in vitro, will be needed as proof.…”

Section: Discussionmentioning

confidence: 99%

“…The symbiosis defect caused by the B. japonicum scoI mutant remained enigmatic (10,21). Other reports have shown, however, that SenC and PrrC play a role in the formation of active cytochrome cbb 3 (22)(23)(24). (iv) A more recently discovered copper chaperone is PCu A C, which rivals Sco1 in its function to metallate the Cu A site.…”

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confidence: 99%

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Copper Starvation-inducible Protein for Cytochrome Oxidase Biogenesis in Bradyrhizobium japonicum

Serventi

Youard

Murset

et al. 2012

Journal of Biological Chemistry

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Background:Copper trafficking in Gram-negative bacteria supplies cuproenzymes via transporters and periplasmic chaperones. Results: Symbiotic nitrogen fixation, denitrification, and copper-starved growth depend on a periplasmic, copper-binding protein named PcuC. Conclusion:The pcuC mutant phenotypes are caused by defects in copper-containing respiratory enzymes. Significance: Research on cytochrome oxidase biogenesis in ␣-proteobacteria, the extant relatives of mitochondria, helps to understand how mitochondria assemble the respiratory chain.

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Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

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Copper Starvation-inducible Protein for Cytochrome Oxidase Biogenesis in Bradyrhizobium japonicum

Serventi

Youard

Murset

et al. 2012

Journal of Biological Chemistry

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“…The CcoO and CcoP subunits are matured via the Ccm pathway, while the heme b 3 -Cu B center of the catalytic subunit CcoN relies on a less-wellunderstood pathway for insertion of heme b and Cu cofactors (7). The similarities of the cbb 3 -Cox phenotypes of CcoA (11), SenC (33), and CcoI (23) mutants and their plausible link(s) to cellular Cu traffic suggest that mutants lacking the Cu atom of CcoN induce degradation of the c-type cytochrome subunits of the enzyme, unlike CcoS mutants that lack both the heme b and the Cu atom of CcoN (23).…”

Section: Discussionmentioning

confidence: 99%

Missense Mutations in Cytochrome c Maturation Genes Provide New Insights into Rhodobacter capsulatus cbb ₃ -Type Cytochrome c Oxidase Biogenesis

et al. 2013

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bThe Rhodobacter capsulatus cbb 3 -type cytochrome c oxidase (cbb 3 -Cox) belongs to the heme-copper oxidase superfamily, and its subunits are encoded by the ccoNOQP operon. Biosynthesis of this enzyme is complex and needs dedicated biogenesis genes (ccoGHIS). It also relies on the c-type cytochrome maturation (Ccm) process, which requires the ccmABCDEFGHI genes, because two of the cbb 3 -Cox subunits (CcoO and CcoP) are c-type cytochromes. Recently, we reported that mutants lacking CcoA, a major facilitator superfamily type transporter, produce very small amounts of cbb 3 -Cox unless the growth medium is supplemented with copper. In this work, we isolated "Cu-unresponsive" derivatives of a ccoA deletion strain that exhibited no cbb 3 -Cox activity even upon Cu supplementation. Molecular characterization of these mutants revealed missense mutations in the ccmA or ccmF gene, required for the Ccm process. As expected, Cu-unresponsive mutants lacked the CcoO and CcoP subunits due to Ccm defects, but remarkably, they contained the CcoN subunit of cbb 3 -Cox. Subsequent construction and examination of single ccm knockout mutants demonstrated that membrane insertion and stability of CcoN occurred in the absence of the Ccm process. Moreover, while the ccm knockout mutants were completely incompetent for photosynthesis, the Cu-unresponsive mutants grew photosynthetically at lower rates and produced smaller amounts of cytochromes c 1 and c 2 than did a wild-type strain due to their restricted Ccm capabilities. These findings demonstrate that different levels of Ccm efficiency are required for the production of various c-type cytochromes and reveal for the first time that maturation of the heme-Cu-containing subunit CcoN of R. capsulatus cbb 3 -Cox proceeds independently of that of the c-type cytochromes during the biogenesis of this enzyme.

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“…The cbb 3 Cox assembly defect in the absence of SenC can be abolished by the addition of least 0.5 μ M Cu. From these and other observations it is concluded that SenC interacts directly with cbb 3 Cox and that it is linked to the Cu delivery pathway to the catalytic CcoN subunit [Banci et al, 2005;Lohmeyer et al, 2012].…”

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confidence: 99%

The Intracytoplasmic Membranes of Purple Bacteria - Assembly of Energy-Transducing Complexes

Drews

2013

Microb Physiol

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The growth of purple bacteria is supported either by a photosynthetic, light-dependent electron transfer system or by a respiratory electron transfer system. Both systems are localized in both a cytoplasmic and an intracytoplasmic membrane system. Formation of the functional complexes is regulated by the oxygen partial pressure and light intensity. The organization and the multistep process of assembly of their components will be described in this review. Most details about the assembly of the respiratory complexes are known.

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The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb3-type cytochrome oxidase in Rhodobacter capsulatus

Cited by 39 publications

References 60 publications

Copper Starvation-inducible Protein for Cytochrome Oxidase Biogenesis in Bradyrhizobium japonicum

Copper Starvation-inducible Protein for Cytochrome Oxidase Biogenesis in Bradyrhizobium japonicum

Missense Mutations in Cytochrome c Maturation Genes Provide New Insights into Rhodobacter capsulatus cbb ₃ -Type Cytochrome c Oxidase Biogenesis

The Intracytoplasmic Membranes of Purple Bacteria - Assembly of Energy-Transducing Complexes

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The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb3-type cytochrome oxidase in Rhodobacter capsulatus

Cited by 39 publications

References 60 publications

Copper Starvation-inducible Protein for Cytochrome Oxidase Biogenesis in Bradyrhizobium japonicum

Copper Starvation-inducible Protein for Cytochrome Oxidase Biogenesis in Bradyrhizobium japonicum

Missense Mutations in Cytochrome c Maturation Genes Provide New Insights into Rhodobacter capsulatus cbb 3 -Type Cytochrome c Oxidase Biogenesis

The Intracytoplasmic Membranes of Purple Bacteria - Assembly of Energy-Transducing Complexes

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Missense Mutations in Cytochrome c Maturation Genes Provide New Insights into Rhodobacter capsulatus cbb ₃ -Type Cytochrome c Oxidase Biogenesis