The interplay between the disulfide bond formation pathway and cytochrome <i>c</i> maturation in <i>Escherichia coli</i>

Mavridou, Despoina A. I.; Ferguson, Stuart J.; Stevens, Julie M.

doi:10.1016/j.febslet.2012.04.055

Cited by 23 publications

(22 citation statements)

References 51 publications

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“…We found that absence of DsbA or DsbB suppresses Ccm deficiency of R. capsulatus CcdA-null [96, 98] or CcmG-null mutants [93], indicating that thioreduction via CcdA-CcmG is dispensable for Ccm in the absence of thio-oxidation by DsbA-DsbB [93]. Similar findings were also shown recently with E. coli [100], reinforcing the proposal that DsbA-DsbB and CcdA-CcmG form a thioredox loop (Fig. 4A).…”

Section: Ccm-system I: Functional Organizationsupporting

confidence: 81%

“…Addition of exogenous thiol compounds is able to alleviate the Ccm deficiency in CcmG and CcdA mutants, confirming their roles in maintaining reduced the apocyt c heme-binding site thiol groups [84, 93, 95, 96]. In the absence of DsbA-DsbB, production of cyts c is decreased but not completely abolished, and in some cases, this can be rescued by addition of oxidants [93, 96–100]. We found that absence of DsbA or DsbB suppresses Ccm deficiency of R. capsulatus CcdA-null [96, 98] or CcmG-null mutants [93], indicating that thioreduction via CcdA-CcmG is dispensable for Ccm in the absence of thio-oxidation by DsbA-DsbB [93].…”

Section: Ccm-system I: Functional Organizationmentioning

confidence: 90%

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Cytochrome c biogenesis System I: An intricate process catalyzed by a maturase supercomplex?

Verissimo

Daldal

2014

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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Cytochromes c are ubiquitous heme proteins that are found in most living organisms and are essential for various energy production pathways as well as other cellular processes. Their biosynthesis relies on a complex post-translational process, called cytochrome c biogenesis, responsible for the formation of stereo-specific thioether bonds between the vinyl groups of heme b (protoporphyrin IX-Fe) and the thiol groups of apocytochromes c heme-binding site (C1XXC2H) cysteine residues. In some organisms this process involves up to nine (CcmABCDEFGHI) membrane proteins working together to achieve heme ligation, designated the Cytochrome c maturation (Ccm)-System I. Here, we review recent findings related to the Ccm-System I found in bacteria, archaea and plant mitochondria, with an emphasis on protein interactions between the Ccm components and their substrates (apocytochrome c and heme). We discuss the possibility that the Ccm proteins may form a multi subunit supercomplex (dubbed “Ccm machine”), and based on the currently available data, we present an updated version of a mechanistic model for Ccm.

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Section: Ccm-system I: Functional Organizationsupporting

confidence: 81%

Section: Ccm-system I: Functional Organizationmentioning

confidence: 90%

Cytochrome c biogenesis System I: An intricate process catalyzed by a maturase supercomplex?

Verissimo

Daldal

2014

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…The simplest explanation for this observation is that iron chelation is a common component of the Cpx-inducing signal. Disruptions in disulfide bond formation in the periplasm (expected in the presence of diamide, a dsbD mutation, or CuSO 4 [24]) lead to defects in the ligation of iron-containing heme B to apocytochrome c (86)(87)(88). V. cholerae is predicted to have 14 ctype cytochromes in the cell envelope (89).…”

Section: Discussionmentioning

confidence: 99%

The Vibrio cholerae Cpx Envelope Stress Response Senses and Mediates Adaptation to Low Iron

2014

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The Cpx pathway, a two-component system that employs the sensor histidine kinase CpxA and the response regulator CpxR, regulates crucial envelope stress responses across bacterial species and affects antibiotic resistance. To characterize the CpxR regulon in Vibrio cholerae, the transcriptional profile of the pandemic V. cholerae El Tor C6706 strain was examined upon overexpression of cpxR. Our data show that the Cpx regulon of V. cholerae is enriched in genes encoding membrane-localized and transport proteins, including a large number of genes known or predicted to be iron regulated. Activation of the Cpx pathway further led to the expression of TolC, the major outer membrane pore, and of components of two RND efflux systems in V. cholerae. We show that iron chelation, toxic compounds, or deletion of specific RND efflux components leads to Cpx pathway activation. Furthermore, mutations that eliminate the Cpx response or members of its regulon result in growth phenotypes in the presence of these inducers that, together with Cpx pathway activation, are partially suppressed by iron. Cumulatively, our results suggest that a major function of the Cpx response in V. cholerae is to mediate adaptation to envelope perturbations caused by toxic compounds and the depletion of iron. Perturbations of the bacterial cell envelope can induce cell envelope stress responses. During this process, signal transduction pathways, such as two-component systems (TCS), are necessary for transducing the information from the cell envelope to the cytoplasm for gene expression regulation (1). TCS are the most prevalent signaling pathways in bacteria, and they are involved in the responses to different inducing cues, mainly related to stress responses and environmental changes (2). The Cpx envelope stress response is an example of a TCS and is composed of the sensor histidine kinase CpxA and the response regulator CpxR (3). This system senses envelope stress and regulates the expression of genes involved in maintaining cell envelope homeostasis to increase bacterial survival under adverse conditions (4).CpxA is an inner membrane (IM) protein that autophosphorylates upon detecting an inducing cue and then becomes a phosphodonor and transfers a phosphoryl group to a conserved aspartate of its response regulator, CpxR (3, 5). CpxR phosphorylation leads to the alteration in transcription of multiple genes by the direct binding of CpxR to DNA (5, 6). In addition, CpxR phosphorylation is modulated indirectly by a periplasmic protein, CpxP, which reduces CpxA activity (6, 7) through a possible direct interaction with the periplasmic sensing domain of CpxA (8-11).The Cpx system in Escherichia coli senses misfolded proteins in the bacterial cell envelope and regulates protein folding and degrading factors, such as DegP, DsbA, and PpiD, involved in the alleviation of the envelope stress (12-15). For example, some of the inducing cues of this pathway are aggregated uropathogenic E. coli P pilus subunits and subunits of the enteropathogenic E. coli bund...

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“…DsbA has a broad substrate specificity, with an estimated 300 substrates in E. coli (2), and homologs of DsbA appear to be widely distributed among Gram-negative bacteria (1,4). Additional components of the pathway include a disulfide isomerase, DsbC, and its redox partner DsbD (5, 6) as well as a reductase, DsbE (CcmG), that also partners with DsbD and functions to reduce the cysteines in apocytochrome c to enable heme to bind (5,7).…”

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confidence: 99%

Functional Analysis of Paralogous Thiol-disulfide Oxidoreductases in Streptococcus gordonii

Davey

Halperin

et al. 2013

Journal of Biological Chemistry

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Background: Thiol-disulfide oxidoreductases catalyze disulfide bond formation in extracellular proteins. Results: A new oxidoreductase, SdbA, affects multiple phenotypes in Streptococcus gordonii and is required for production of disulfide-bonded proteins. Conclusion: SdbA is a new type of oxidoreductase that has important biological functions. Significance: This is the first indication that thiol-disulfide oxidoreductases are important to the physiology of Firmicute bacteria.

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The interplay between the disulfide bond formation pathway and cytochrome c maturation in Escherichia coli

Cited by 23 publications

References 51 publications

Cytochrome c biogenesis System I: An intricate process catalyzed by a maturase supercomplex?

Cytochrome c biogenesis System I: An intricate process catalyzed by a maturase supercomplex?

The Vibrio cholerae Cpx Envelope Stress Response Senses and Mediates Adaptation to Low Iron

Functional Analysis of Paralogous Thiol-disulfide Oxidoreductases in Streptococcus gordonii

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