Four genes are required for the system II cytochrome <i>c</i> biogenesis pathway in <i>Bordetella pertussis</i>, a unique bacterial model

Beckett, Caroline S.; Loughman, Jennifer A.; Karberg, Katherine A.; Donato, Gina M.; Goldman, William E.; Kranz, Robert G.

doi:10.1046/j.1365-2958.2000.02174.x

Cited by 80 publications

(88 citation statements)

References 52 publications

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“…The transposon in mutant W3 was located in ORF SMc00248, which has been annotated as ccsA (Galibert et al, 2001), a gene involved in type II cytochrome c maturation (Beckett et al, 2000;Hamel et al, 2003). However, the protein predicted from SMc00248 showed 49 % identity and 65 % similarity over its entire length to Rhodobacter capsulatus CcdA (accession no.…”

Section: Isolation Of S Meliloti Nadi " Mutants and Localization Of mentioning

confidence: 99%

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

et al. 2007

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Section: Isolation Of S Meliloti Nadi " Mutants and Localization Of mentioning

confidence: 99%

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

et al. 2007

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“…HCF164 displays similarity to CcsX/ResA, a thioredoxin-like protein involved in system II bacterial cytochrome c assembly pathway (63,64). Remarkably, CcsX, ResA, and HCF164 proteins share the same membrane topology with the thioredoxinlike domain facing the p-side of the membrane, suggesting that their relevant targets of action are also located in this compartment (62)(63)(64). The definitive placement of HCF164 in plastid cytochrome c maturation is still uncertain because the defect in cytochrome b 6 f assembly could not be localized specifically to a block in the maturation of a particular subunit (i.e.…”

Section: Figmentioning

confidence: 99%

“…These redox components might correspond to the gene products of CCS4 and CCS5 loci in Chlamydomonas (17,20). Indeed, a preliminary functional assessment of these genes in redox chemistry is based on the observation that ccs4 and ccs5 mutants, similar to ccda and resA/ccsx mutants in bacteria (26,28,63,64), can be rescued for cytochrome c deficiency by exogenous reduced thiol compounds. 9 It is conceivable that, because of the compartmentalization of the thylakoid lumen, the redox pathway evolved in plastids relies on several players (at least CCDA, HCF164, Ccs4, and Ccs5) and is therefore more complex than its bacterial counterpart.…”

Section: Figmentioning

confidence: 99%

A Homolog of Prokaryotic Thiol Disulfide Transporter CcdA Is Required for the Assembly of the Cytochrome bf Complex in Arabidopsis Chloroplasts

Page¹,

Hamel²,

Gabilly³

et al. 2004

Journal of Biological Chemistry

101

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The c-type cytochromes are defined by the occurrence of heme covalently linked to the polypeptide via thioether bonds between heme and the cysteine sulfhydryls in the CXXCH motif of apocytochrome. Maintenance of apocytochrome sulfhydryls in a reduced state is a prerequisite for covalent ligation of heme to the CXXCH motif. In bacteria, a thiol disulfide transporter and a thioredoxin are two components in a thio-reduction pathway involved in c-type cytochrome assembly. We have identified in photosynthetic eukaryotes nucleus-encoded homologs of a prokaryotic thiol disulfide transporter, CcdA, which all display an N-terminal extension with respect to their bacterial counterparts. The extension of Arabidopsis CCDA functions as a targeting sequence, suggesting a plastid site of action for CCDA in eukaryotes. Using PhoA and LacZ as topological reporters, we established that Arabidopsis CCDA is a polytopic protein with within-membrane strictly conserved cysteine residues. Insertional mutants in the Arabidopsis CCDA gene were identified, and loss-of-function alleles were shown to impair photosynthesis because of a defect in cytochrome b 6 f accumulation, which we attribute to a block in the maturation of holocytochrome f, whose heme binding domain resides in the thylakoid lumen. We postulate that plastid cytochrome c maturation requires CCDA, thioredoxin HCF164, and other molecules in a membrane-associated trans-thylakoid thiol-reducing pathway.The c-type cytochromes are a virtually ubiquitous yet rather structurally diverse group of hemoproteins that reside on the so-called p-side 1 of the energy-transducing membrane systems where they function typically as electron carriers (1, 2). The c-type cytochromes are defined by the occurrence of heme covalently attached to the polypeptide via two thioether linkages between the vinyl groups of heme and the cysteine sulfhydryls in the apocytochrome (1, 3). A CXXCH 2 sequence in the apocytochrome provides the thiols for formation of the thioether bonds, and the imidazole of the histidine residue serves as one of the axial ligands of the heme. Remarkably, three distinct assembly pathways, referred to as systems I, II, and III, have emerged through genetic analysis of c-type cytochrome maturation in bacteria, chloroplasts, and mitochondria (for review, see Refs. 1 and 4 -7), an unexpected finding for what appears on the surface to be a rather simple chemical reaction (i.e. the addition of apocytochrome cysteine thiols to the vinyls of heme). Each system can be distinguished on the basis of a sequence relationship of specific assembly factors. Yet, there is an underlying assumption that the three systems are united by common biochemical requirements for holocytochrome c biogenesis (for review, see Refs. 2, 4, and 8). For instance, the need for reducing conditions appears to be inherent to the chemistry of thioether bond formation (4). Both substrates, apocytochrome c sulfhydryls and heme, need to be maintained reduced prior to the ligation of heme as indicated from in vitro and in o...

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“…Remarkably, however, system II seems to comprise just three, rather than eight or nine, CCMspecific proteins (19,38,39). The type II system of Bacillus subtilis (Fig.…”

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confidence: 99%

Structural Basis of Redox-coupled Protein Substrate Selection by the Cytochrome c Biosynthesis Protein ResA

Crow

Acheson

Brun

et al. 2004

Journal of Biological Chemistry

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Post-translational maturation of cytochromes c involves the covalent attachment of heme to the Cys-XxxXxx-Cys-His motif of the apo-cytochrome. For this process, the two cysteines of the motif must be in the reduced state. In bacteria, this is achieved by dedicated, membrane-bound thiol-disulfide oxidoreductases with a high reducing power, which are essential components of cytochrome c maturation systems and are also linked to cellular disulfide-bond formation machineries. Here we report high-resolution structures of oxidized and reduced states of a soluble, functional domain of one such oxidoreductase, ResA, from Bacillus subtilis. The structures elucidate the structural basis of the protein's high reducing power and reveal the largest redox-coupled conformational changes observed to date in any thioredoxin-like protein. These redox-coupled changes alter the protein surface and illustrate how the redox state of ResA predetermines to which substrate it binds. Furthermore, a polar cavity, present only in the reduced state, may confer specificity to recognize apo-cytochrome c. The described features of ResA are likely to be general for bacterial cytochrome c maturation systems.

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Four genes are required for the system II cytochrome c biogenesis pathway in Bordetella pertussis, a unique bacterial model

Cited by 80 publications

References 52 publications

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

A Homolog of Prokaryotic Thiol Disulfide Transporter CcdA Is Required for the Assembly of the Cytochrome bf Complex in Arabidopsis Chloroplasts

Structural Basis of Redox-coupled Protein Substrate Selection by the Cytochrome c Biosynthesis Protein ResA

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