Roles of the ccoGHIS gene products in the biogenesis of the cbb3-type cytochrome c oxidase

Koch, Hans‐Georg; Winterstein, Christine; Sarıbaş, A. Sami; Alben, James O.; Daldal, Fevzi

doi:10.1006/jmbi.2000.3555

Cited by 88 publications

(180 citation statements)

References 53 publications

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“…Finally, the combination of CX 3 CP motifs and a polyferredoxin module is found in other redox proteins with putative regulatory or sensory functions (3,4,9,22,23,28,30,32,36,38,39). A mechanistic understanding of this structure will therefore have an impact on many metabolic systems, including N 2 O respiration.…”

Section: Discussionmentioning

confidence: 99%

Functional Domains of NosR, a Novel Transmembrane Iron-Sulfur Flavoprotein Necessary for Nitrous Oxide Respiration

Wunsch

Zumft

2005

J Bacteriol

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Bacterial nitrous oxide (N 2 O) respiration depends on the polytopic membrane protein NosR for the expression of N 2 O reductase from the nosZ gene. We constructed His-tagged NosR and purified it from detergentsolubilized membranes of Pseudomonas stutzeri ATCC 14405. NosR is an iron-sulfur flavoprotein with redox centers positioned at opposite sides of the cytoplasmic membrane. The flavin cofactor is presumably bound covalently to an invariant threonine residue of the periplasmic domain. NosR also features conserved CX 3 CP motifs, located C-terminally of the transmembrane helices TM4 and TM6. We genetically manipulated nosR with respect to these different domains and putative functional centers and expressed recombinant derivatives in a nosR null mutant, MK418nosR::Tn5. NosR's function was studied by its effects on N 2 O respiration, NosZ synthesis, and the properties of purified NosZ proteins. Although all recombinant NosR proteins allowed the synthesis of NosZ, a loss of N 2 O respiration was observed upon deletion of most of the periplasmic domain or of the C-terminal parts beyond TM2 or upon modification of the cysteine residues in a highly conserved motif, CGWLCP, following TM4. Nonetheless, NosZ purified from the recombinant NosR background exhibited in vitro catalytic activity. Certain NosR derivatives caused an increase in NosZ of the spectral contribution from a modified catalytic Cu site. In addition to its role in nosZ expression, NosR supports in vivo N 2 O respiration. We also discuss its putative functions in electron donation and redox activation.

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Section: Discussionmentioning

confidence: 99%

Functional Domains of NosR, a Novel Transmembrane Iron-Sulfur Flavoprotein Necessary for Nitrous Oxide Respiration

Wunsch

Zumft

2005

J Bacteriol

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“…When cells were grown in BG-11-C medium, cytochrome oxidase activities were lower (mean 58%) in membranes from Synechocystis PCC 6803(ctaA) compared with wild type in each of eight independent experiments. It is noted that a related copper transporter has recently been implicated in the biogenesis of cytochrome c oxidase in Rhodobacter capsulatus (26). …”

Section: Photooxidation Of Cytochrome C 6 (Petj) In Copper-containingmentioning

confidence: 99%

Two Menkes-type ATPases Supply Copper for Photosynthesis inSynechocystis PCC 6803

Tottey¹,

Rich

Rondet³

et al. 2001

Journal of Biological Chemistry

141

190

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Synechocystis PCC 6803 contains four genes encoding polypeptides with sequence features of CPx-type ATPases, two of which are now designated pacS and ctaA. We show that CtaA and PacS (but not the related transporters, ZiaA or CoaT) facilitate switching to the use of copper (in plastocyanin) as an alternative to iron (in cytochrome c 6 ) for the carriage of electrons within the thylakoid lumen. Disruption of pacS reduced copper tolerance but enhanced silver tolerance, and pacS-mediated restoration of copper tolerance was used to select transformants. Disruption of ctaA caused no change in copper tolerance but reduced the amount of copper cell ؊1 . In cultures supplemented with 0.2 M copper, photooxidation of cytochrome c 6 (PetJ) was depressed in wild-type cells but remained elevated in both Synechocystis PCC 6803(ctaA) and Synechocystis PCC 6803(pacS). Conversely, plastocyanin transcripts (petE) were less abundant in both mutants at this [copper]. Synechocystis PCC 6803(ctaA) and Synechocystis PCC 6803(pacS) showed increased iron dependence with impaired growth in deferoxamine mesylate (iron chelator)-containing media. Double mutants also deficient in cytochrome c 6 , Synechocystis PCC 6803(petJ,ctaA) and Synechocystis PCC 6803(petJ,pacS), were viable, but the former had increased copper dependence with severely impaired growth in the presence of bathocuproinedisulfonic acid (copper chelator). Analogous transporters are likely to supply copper to plastocyanin in chloroplasts.

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“…The biogenesis of cbb 3 was mainly studied in Rhodobacter capsulatus and in Bradyrhizobium japonicum. In both strains, the ccoGHIS (fixGHIS) gene cluster was shown to be required for the formation of a functional cbb 3 (7,8). In Rhodobacter capsulatus it was suggested that CcoS is involved in the maturation of the CcoN Cu B -b 3 center.…”

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confidence: 99%

“…SenC, a homologue of Sco1, is also required for the assembly of an active cbb 3 complex in R. capsulatus (9). CcoI, a member of P1B-type ATPase, is required for a normal amount of active cbb 3 complex in both R. capsulatus and B. japonicum (8,10).…”

mentioning

confidence: 99%

CtpA, a Copper-translocating P-type ATPase Involved in the Biogenesis of Multiple Copper-requiring Enzymes

Hassani

Astier

Nitschke

et al. 2010

Journal of Biological Chemistry

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The ctpA (ccoI) gene product, a putative inner membrane copper-translocating P1B-type ATPase present in many bacteria, has been shown to be involved only in the cbb 3 assembly in Rhodobacter capsulatus and Bradyrhizobium japonicum. ctpA was disrupted in Rubrivivax gelatinosus, and the mutants showed a drastic decrease in both cbb 3 and caa 3 oxidase activities. Inactivation of ctpA results also in a decrease in the amount of the nitrous oxide reductase, NosZ. This pleiotropic phenotype could be partially rescued by excess copper in the medium, indicating that CtpA is likely a copper transporter that supplies copper-requiring proteins in the membrane with this metal. Although CtpA shares significant sequence homologies with the homeostasis copper efflux P1B-type ATPases including the bacterial CopA and the human ATP7A and ATP7B, disruption of ctpA did not result in any sensitivity to excess copper. This indicates that the CtpA is not crucial for copper tolerance but is involved in the assembly of membrane and periplasmic copper enzymes in this bacterium. The potential roles of CtpA in bacteria in comparison with CopA are discussed.

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Roles of the ccoGHIS gene products in the biogenesis of the cbb3-type cytochrome c oxidase

Cited by 88 publications

References 53 publications

Functional Domains of NosR, a Novel Transmembrane Iron-Sulfur Flavoprotein Necessary for Nitrous Oxide Respiration

Functional Domains of NosR, a Novel Transmembrane Iron-Sulfur Flavoprotein Necessary for Nitrous Oxide Respiration

Two Menkes-type ATPases Supply Copper for Photosynthesis inSynechocystis PCC 6803

CtpA, a Copper-translocating P-type ATPase Involved in the Biogenesis of Multiple Copper-requiring Enzymes

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