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Journal articles on the topic 'DsbD'

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Published: 10 December 2022

Last updated: 29 July 2024

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1

Cho, Seung-Hyun, and Jon Beckwith. "Mutations of the Membrane-Bound Disulfide Reductase DsbD That Block Electron Transfer Steps from Cytoplasm to Periplasm in Escherichia coli." Journal of Bacteriology 188, no. 14 (July 15, 2006): 5066–76. http://dx.doi.org/10.1128/jb.00368-06.

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ABSTRACT The cytoplasmic membrane protein DsbD keeps the periplasmic disulfide isomerase DsbC reduced, using the cytoplasmic reducing power of thioredoxin. DsbD contains three domains, each containing two reactive cysteines. One membrane-embedded domain, DsbDβ, transfers electrons from thioredoxin to the carboxy-terminal thioredoxin-like periplasmic domain DsbDγ. To evaluate the role of conserved amino acid residues in DsbDβ in the electron transfer process, we substituted alanines for each of 19 conserved amino acid residues and assessed the in vivo redox states of DsbC and DsbD. The mutant DsbDs of 11 mutants which caused defects in DsbC reduction showed relatively oxidized redox states. To analyze the redox state of each DsbD domain, we constructed a thrombin-cleavable DsbD (DsbDTH) from which we could generate all three domains as separate polypeptide chains by thrombin treatment in vitro. We divided the mutants with strong defects into two classes. The first mutant class consists of mutant DsbDβ proteins that cannot receive electrons from cytoplasmic thioredoxin, resulting in a DsbD that has all six of its cysteines disulfide bonded. The second mutant class represents proteins in which the transfer of electrons from DsbDβ to DsbDγ appears to be blocked. This class includes the mutant with the most clear-cut defect, P284A. We relate the properties of the mutants to the positions of the amino acids in the structure of DsbD and discuss mechanisms that would interfere with the electron transfer process.

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2

Walden, Patricia M., Andrew E. Whitten, Lakshmanane Premkumar, Maria A. Halili, Begoña Heras, Gordon J. King, and Jennifer L. Martin. "The atypical thiol–disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase." Acta Crystallographica Section D Structural Biology 75, no. 3 (February 26, 2019): 283–95. http://dx.doi.org/10.1107/s2059798318018442.

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Disulfide-bond-forming (DSB) oxidative folding enzymes are master regulators of virulence that are localized to the periplasm of many Gram-negative bacteria. The archetypal DSB machinery from Escherichia coli K-12 consists of a dithiol-oxidizing redox-relay pair (DsbA/B), a disulfide-isomerizing redox-relay pair (DsbC/D) and the specialist reducing enzymes DsbE and DsbG that also interact with DsbD. By contrast, the Gram-negative bacterium Wolbachia pipientis encodes just three DSB enzymes. Two of these, α-DsbA1 and α-DsbB, form a redox-relay pair analogous to DsbA/B from E. coli. The third enzyme, α-DsbA2, incorporates a DsbA-like sequence but does not interact with α-DsbB. In comparison to other DsbA enzymes, α-DsbA2 has ∼50 extra N-terminal residues (excluding the signal peptide). The crystal structure of α-DsbA2ΔN, an N-terminally truncated form in which these ∼50 residues are removed, confirms the DsbA-like nature of this domain. However, α-DsbA2 does not have DsbA-like activity: it is structurally and functionally different as a consequence of its N-terminal residues. Firstly, α-DsbA2 is a powerful disulfide isomerase and a poor dithiol oxidase: i.e. its role is to shuffle rather than to introduce disulfide bonds. Moreover, small-angle X-ray scattering (SAXS) of α-DsbA2 reveals a homotrimeric arrangement that differs from those of the other characterized bacterial disulfide isomerases DsbC from Escherichia coli (homodimeric) and ScsC from Proteus mirabilis (PmScsC; homotrimeric with a shape-shifter peptide). α-DsbA2 lacks the shape-shifter motif and SAXS data suggest that it is less flexible than PmScsC. These results allow conclusions to be drawn about the factors that are required for functionally equivalent disulfide isomerase enzymatic activity across structurally diverse protein architectures.

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3

Lin, Dongxia, Byoungkwan Kim, and James M. Slauch. "DsbL and DsbI contribute to periplasmic disulfide bond formation in Salmonella enterica serovar Typhimurium." Microbiology 155, no. 12 (December 1, 2009): 4014–24. http://dx.doi.org/10.1099/mic.0.032904-0.

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Disulfide bond formation in periplasmic proteins is catalysed by the DsbA/DsbB system in most Gram-negative bacteria. Salmonella enterica serovar Typhimurium also encodes a paralogous pair of proteins to DsbA and DsbB, DsbL and DsbI, respectively, downstream of a periplasmic arylsulfate sulfotransferase (ASST). We show that DsbL and DsbI function as a redox pair contributing to periplasmic disulfide bond formation and, as such, affect transcription of the Salmonella pathogenicity island 1 (SPI1) type three secretion system genes and activation of the RcsCDB system, as well as ASST activity. In contrast to DsbA/DsbB, however, the DsbL/DsbI system cannot catalyse the disulfide bond formation required for flagellar assembly. Phylogenic analysis suggests that the assT dsbL dsbI genes are ancestral in the Enterobacteriaceae, but have been lost in many lineages. Deletion of assT confers no virulence defect during acute Salmonella infection of mice.

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4

Skórko-Glonek, Joanna, Anna Sobiecka-Szkatuła, and Barbara Lipińska. "Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli." Acta Biochimica Polonica 53, no. 3 (October 1, 2006): 585–89. http://dx.doi.org/10.18388/abp.2006_3331.

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DsbA is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envelope. In the present work we provided the first detailed characterization of disulfide exchange between DsbA and its natural substrate, HtrA protease. We demonstrated that HtrA oxidation relies on DsbA, both in vivo and in vitro. We followed the disulfide exchange between these proteins spectrofluorimetrically and found that DsbA oxidizes HtrA with a 1:1 stoichiometry. The calculated second-order apparent rate constant (kapp) of this reaction was 3.3x10(4)+/-0.6x10(4) M-1s-1. This value was significantly higher than the values obtained for nonfunctional disulfide exchanges between DsbA and DsbC or DsbD and it was comparable to the kapp values calculated for in vitro oxidation of certain non-natural DsbA substrates of eukaryotic origin.

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5

Kurokawa, Yoichi, Hideki Yanagi, and Takashi Yura. "Overexpression of Protein Disulfide Isomerase DsbC Stabilizes Multiple-Disulfide-Bonded Recombinant Protein Produced and Transported to the Periplasm in Escherichia coli." Applied and Environmental Microbiology 66, no. 9 (September 1, 2000): 3960–65. http://dx.doi.org/10.1128/aem.66.9.3960-3965.2000.

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ABSTRACT Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm ofEscherichia coli. By using a set of Dsb coexpression plasmids constructed recently, we analyzed the effects of Dsb overexpression on production of horseradish peroxidase (HRP) isozyme C that contains complex disulfide bonds and tends to aggregate when produced in E. coli. When transported to the periplasm, HRP was unstable but was markedly stabilized upon simultaneous overexpression of the set of Dsb proteins (DsbABCD). Whereas total HRP production increased severalfold upon overexpression of at least disulfide-bonded isomerase DsbC, maximum transport of HRP to the periplasm seemed to require overexpression of all DsbABCD proteins, suggesting that excess Dsb proteins exert synergistic effects in assisting folding and transport of HRP. Periplasmic production of HRP also increased when calcium, thought to play an essential role in folding of nascent HRP polypeptide, was added to the medium with or without Dsb overexpression. These results suggest that Dsb proteins and calcium play distinct roles in periplasmic production of HRP, presumably through facilitating correct folding. The present Dsb expression plasmids should be useful in assessing and dissecting periplasmic production of proteins that contain multiple disulfide bonds in E. coli.

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6

Goldstone, D., P. W. Haebel, F. Katzen, M. W. Bader, J. C. A. Bardwell, J. Beckwith, and P. Metcalf. "DsbC activation by the N-terminal domain of DsbD." Proceedings of the National Academy of Sciences 98, no. 17 (August 7, 2001): 9551–56. http://dx.doi.org/10.1073/pnas.171315498.

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7

Smith, Roxanne P., Biswaranjan Mohanty, Shakeel Mowlaboccus, Jason J. Paxman, Martin L. Williams, Stephen J. Headey, Geqing Wang, et al. "Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens." Journal of Biological Chemistry 293, no. 43 (September 4, 2018): 16559–71. http://dx.doi.org/10.1074/jbc.ra118.004847.

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The worldwide incidence of neisserial infections, particularly gonococcal infections, is increasingly associated with antibiotic-resistant strains. In particular, extensively drug-resistant Neisseria gonorrhoeae strains that are resistant to third-generation cephalosporins are a major public health concern. There is a pressing clinical need to identify new targets for the development of antibiotics effective against Neisseria-specific processes. In this study, we report that the bacterial disulfide reductase DsbD is highly prevalent and conserved among Neisseria spp. and that this enzyme is essential for survival of N. gonorrhoeae. DsbD is a membrane-bound protein that consists of two periplasmic domains, n-DsbD and c-DsbD, which flank the transmembrane domain t-DsbD. In this work, we show that the two functionally essential periplasmic domains of Neisseria DsbD catalyze electron transfer reactions through unidirectional interdomain interactions, from reduced c-DsbD to oxidized n-DsbD, and that this process is not dictated by their redox potentials. Structural characterization of the Neisseria n- and c-DsbD domains in both redox states provides evidence that steric hindrance reduces interactions between the two periplasmic domains when n-DsbD is reduced, thereby preventing a futile redox cycle. Finally, we propose a conserved mechanism of electron transfer for DsbD and define the residues involved in domain–domain recognition. Inhibitors of the interaction of the two DsbD domains have the potential to be developed as anti-neisserial agents.

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8

Yu, Jun. "Inactivation of DsbA, but Not DsbC and DsbD, Affects the Intracellular Survival and Virulence ofShigella flexneri." Infection and Immunity 66, no. 8 (August 1, 1998): 3909–17. http://dx.doi.org/10.1128/iai.66.8.3909-3917.1998.

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ABSTRACT In this study, three mutants,dsbA::kan, dsbC-kan, anddsbD-kan, of Shigella flexneri serotype 5 were constructed and characterized to investigate the role of the periplasmic thiol:disulfide oxidoreductases in pathogenicity. In gentamicin protection assays and the Serény test, thedsbA mutant showed reduced virulence while thedsbC and dsbD mutants were similar to the wild type. That inactivation of dsbA was responsible for the reduced virulence was verified by complementation with the cloned wild-type gene in in vitro and in vivo assays. Despite the changed virulence behavior, the dsbA mutant could penetrate HeLa cells 15 min postinfection, consistent with the fact that it actively secretes Ipa proteins upon Congo red induction. Furthermore, thedsbA mutant was able to produce actin comets and protrusions, indicating its capacity for intra- and intercellular spread. However, a kinetic analysis of intracellular growth showed that the dsbA mutant barely grew in HeLa cells during a 4-h infection whereas the wild type had a doubling time of 41 min. Electron microscopy analysis revealed that dsbA mutant bacteria were trapped in protrusion-derived vacuoles surrounded by double membranes, resembling an icsB mutant reported previously. Moreover, the trapped bacteria appeared to be lysed simultaneously with the double membranes, resulting in characteristic empty vacuoles in the host cell cytosol. Thus, the attenuation mechanism for dsbAmutant appears to be more complicated than was previously suggested.

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9

Kimball, Richard A., Laetitia Martin, and Milton H. Saier Jr. "Reversing Transmembrane Electron Flow: The DsbD and DsbB Protein Families." Journal of Molecular Microbiology and Biotechnology 5, no. 3 (2003): 133–49. http://dx.doi.org/10.1159/000070263.

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10

Smith, Roxanne P., Andrew E. Whitten, Jason J. Paxman, Charlene M. Kahler, Martin J. Scanlon, and Begoña Heras. "Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme inNeisseria meningitidis." Acta Crystallographica Section F Structural Biology Communications 74, no. 1 (January 1, 2018): 31–38. http://dx.doi.org/10.1107/s2053230x17017800.

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The membrane protein DsbD is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochromecmaturation and oxidative stress defence. DsbD is a multi-domain protein consisting of a transmembrane domain (t-DsbD) flanked by two periplasmic domains (n-DsbD and c-DsbD). Previous studies have shown that DsbD is required for the survival of the obligate human pathogenNeisseria meningitidis. To help understand the structural and functional aspects ofN. meningitidisDsbD, the two periplasmic domains which are required for electron transfer are being studied. Here, the expression, purification and biophysical properties of n-NmDsbD and c-NmDsbD are described. The crystallization and crystallographic analysis of n-NmDsbD and c-NmDsbD are also described in both redox states, which differ only in the presence or absence of a disulfide bond but which crystallized in completely different conditions. Crystals of n-NmDsbDOx, n-NmDsbDRed, c-NmDsbDOxand c-NmDsbDReddiffracted to 2.3, 1.6, 2.3 and 1.7 Å resolution and belonged to space groupsP213,P321,P41andP1211, respectively.

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11

Bushweller, John H. "Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA." Journal of Molecular Biology 432, no. 18 (August 2020): 5091–103. http://dx.doi.org/10.1016/j.jmb.2020.04.008.

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12

Deshmukh, Meenal, Serdar Turkarslan, Donniel Astor, Maria Valkova-Valchanova, and Fevzi Daldal. "The Dithiol:Disulfide Oxidoreductases DsbA and DsbB of Rhodobacter capsulatus Are Not Directly Involved in Cytochrome c Biogenesis, but Their Inactivation Restores the Cytochrome c Biogenesis Defect of CcdA-Null Mutants." Journal of Bacteriology 185, no. 11 (June 1, 2003): 3361–72. http://dx.doi.org/10.1128/jb.185.11.3361-3372.2003.

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ABSTRACT The cytoplasmic membrane protein CcdA and its homologues in other species, such as DsbD of Escherichia coli, are thought to supply the reducing equivalents required for the biogenesis of c-type cytochromes that occurs in the periplasm of gram-negative bacteria. CcdA-null mutants of the facultative phototroph Rhodobacter capsulatus are unable to grow under photosynthetic conditions (Ps−) and do not produce any active cytochrome c oxidase (Nadi−) due to a pleiotropic cytochrome c deficiency. However, under photosynthetic or respiratory growth conditions, these mutants revert frequently to yield Ps+ Nadi+ colonies that produce c-type cytochromes despite the absence of CcdA. Complementation of a CcdA-null mutant for the Ps+ growth phenotype was attempted by using a genomic library constructed with chromosomal DNA from a revertant. No complementation was observed, but plasmids that rescued a CcdA-null mutant for photosynthetic growth by homologous recombination were recovered. Analysis of one such plasmid revealed that the rescue ability was mediated by open reading frame 3149, encoding the dithiol:disulfide oxidoreductase DsbA. DNA sequence data revealed that the dsbA allele on the rescuing plasmid contained a frameshift mutation expected to produce a truncated, nonfunctional DsbA. Indeed, a dsbA ccdA double mutant was shown to be Ps+ Nadi+, establishing that in R. capsulatus the inactivation of dsbA suppresses the c-type cytochrome deficiency due to the absence of ccdA. Next, the ability of the wild-type dsbA allele to suppress the Ps+ growth phenotype of the dsbA ccdA double mutant was exploited to isolate dsbA-independent ccdA revertants. Sequence analysis revealed that these revertants carried mutations in dsbB and that their Ps+ phenotypes could be suppressed by the wild-type allele of dsbB. As with dsbA, a dsbB ccdA double mutant was also Ps+ Nadi+ and produced c-type cytochromes. Therefore, the absence of either DsbA or DsbB restores c-type cytochrome biogenesis in the absence of CcdA. Finally, it was also found that the DsbA-null and DsbB-null single mutants of R. capsulatus are Ps+ and produce c-type cytochromes, unlike their E. coli counterparts, but are impaired for growth under respiratory conditions. This finding demonstrates that in R. capsulatus the dithiol:disulfide oxidoreductases DsbA and DsbB are not essential for cytochrome c biogenesis even though they are important for respiration under certain conditions.

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13

Hiniker, Annie, Didier Vertommen, James C. A. Bardwell, and Jean-Francois Collet. "Evidence for Conformational Changes within DsbD: Possible Role for Membrane-Embedded Proline Residues." Journal of Bacteriology 188, no. 20 (October 1, 2006): 7317–20. http://dx.doi.org/10.1128/jb.00383-06.

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ABSTRACT The mechanism by which DsbD transports electrons across the cytoplasmic membrane is unknown. Here we provide evidence that DsbD's conformation depends on its oxidation state. Our data also suggest that four highly conserved prolines surrounding DsbD's membrane-embedded catalytic cysteines may have an important functional role, possibly conferring conformational flexibility to DsbD.

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14

Kumar, Pradeep, Soma Sannigrahi, Jessica Scoullar, Charlene M. Kahler, and Yih-Ling Tzeng. "Characterization of DsbD in Neisseria meningitidis." Molecular Microbiology 79, no. 6 (January 24, 2011): 1557–73. http://dx.doi.org/10.1111/j.1365-2958.2011.07546.x.

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15

Feissner, Robert E., Caroline S. Beckett, Jennifer A. Loughman, and Robert G. Kranz. "Mutations in Cytochrome Assembly and Periplasmic Redox Pathways in Bordetella pertussis." Journal of Bacteriology 187, no. 12 (June 15, 2005): 3941–49. http://dx.doi.org/10.1128/jb.187.12.3941-3949.2005.

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ABSTRACT Transposon mutagenesis of Bordetella pertussis was used to discover mutations in the cytochrome c biogenesis pathway called system II. Using a tetramethyl-p-phenylenediamine cytochrome c oxidase screen, 27 oxidase-negative mutants were isolated and characterized. Nine mutants were still able to synthesize c-type cytochromes and possessed insertions in the genes for cytochrome c oxidase subunits (ctaC, -D, and -E), heme a biosynthesis (ctaB), assembly of cytochrome c oxidase (sco2), or ferrochelatase (hemZ). Eighteen mutants were unable to synthesize all c-type cytochromes. Seven of these had transposons in dipZ (dsbD), encoding the transmembrane thioreduction protein, and all seven mutants were corrected for cytochrome c assembly by exogenous dithiothreitol, which was consistent with the cytochrome c cysteinyl residues of the CXXCH motif requiring periplasmic reduction. The remaining 11 insertions were located in the ccsBA operon, suggesting that with the appropriate thiol-reducing environment, the CcsB and CcsA proteins comprise the entire system II biosynthetic pathway. Antiserum to CcsB was used to show that CcsB is absent in ccsA mutants, providing evidence for a stable CcsA-CcsB complex. No mutations were found in the genes necessary for disulfide bond formation (dsbA or dsbB). To examine whether the periplasmic disulfide bond pathway is required for cytochrome c biogenesis in B. pertussis, a targeted knockout was made in dsbB. The DsbB− mutant makes holocytochromes c like the wild type does and secretes and assembles the active periplasmic alkaline phosphatase. A dipZ mutant is not corrected by a dsbB mutation. Alternative mechanisms to oxidize disulfides in B. pertussis are analyzed and discussed.

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16

Rozhkova, Anna, and Rudi Glockshuber. "Thermodynamic Aspects of DsbD-Mediated Electron Transport." Journal of Molecular Biology 380, no. 5 (July 2008): 783–88. http://dx.doi.org/10.1016/j.jmb.2008.05.050.

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17

Brot, Nathan, Jean-François Collet, Lynnette C. Johnson, Thomas J. Jönsson, Herbert Weissbach, and W. Todd Lowther. "The Thioredoxin Domain of Neisseria gonorrhoeae PilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases." Journal of Biological Chemistry 281, no. 43 (August 22, 2006): 32668–75. http://dx.doi.org/10.1074/jbc.m604971200.

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The PilB protein from Neisseria gonorrhoeae is located in the periplasm and made up of three domains. The N-terminal, thioredoxin-like domain (NT domain) is fused to tandem methionine sulfoxide reductase A and B domains (MsrA/B). We show that the α domain of Escherichia coli DsbD is able to reduce the oxidized NT domain, which suggests that DsbD in Neisseria can transfer electrons from the cytoplasmic thioredoxin to the periplasm for the reduction of the MsrA/B domains. An analysis of the available complete genomes provides further evidence for this proposition in other bacteria where DsbD/CcdA, Trx, MsrA, and MsrB gene homologs are all located in a gene cluster with a common transcriptional direction. An examination of wild-type PilB and a panel of Cys to Ser mutants of the full-length protein and the individually expressed domains have also shown that the NT domain more efficiently reduces the MsrA/B domains when in the polyprotein context. Within this frame-work there does not appear to be a preference for the NT domain to reduce the proximal MsrA domain over MsrB domain. Finally, we report the 1.6Å crystal structure of the NT domain. This structure confirms the presence of a surface loop that makes it different from other membrane-tethered, Trx-like molecules, including TlpA, CcmG, and ResA. Subtle differences are observed in this loop when compared with the Neisseria meningitidis NT domain structure. The data taken together supports the formation of specific NT domain interactions with the MsrA/B domains and its in vivo recycling partner, DsbD.

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18

Stenson, Trevor H., and Alison A. Weiss. "DsbA and DsbC Are Required for Secretion of Pertussis Toxin by Bordetella pertussis." Infection and Immunity 70, no. 5 (May 2002): 2297–303. http://dx.doi.org/10.1128/iai.70.5.2297-2303.2002.

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ABSTRACT The Dsb family of enzymes catalyzes disulfide bond formation in the gram-negative periplasm, which is required for folding and assembly of many secreted proteins. Pertussis toxin is arguably the most complex toxin known: it is assembled from six subunits encoded by five genes (for subunits S1 to S5), with 11 intramolecular disulfide bonds. To examine the role of the Dsb enzymes in assembly and secretion of pertussis toxin, we identified and mutated the Bordetella pertussis dsbA, dsbB, and dsbC homologues. Mutations in dsbA or dsbB resulted in decreased levels of S1 (the A subunit) and S2 (a B-subunit protein), demonstrating that DsbA and DsbB are required for toxin assembly. Mutations in dsbC did not impair assembly of periplasmic toxin but resulted in decreased toxin secretion, suggesting a defect in the formation of the Ptl secretion complex.

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19

Haebel, P. W., D. Goldstone, and P. Metcalf. "The disulfide bond isomerase DsbC is specifically activated by the IG fold domain of the electron transporter DsbD." Acta Crystallographica Section A Foundations of Crystallography 58, s1 (August 6, 2002): c5. http://dx.doi.org/10.1107/s010876730208529x.

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20

REID, Eleanor, Jeff COLE, and Deborah J. EAVES. "The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly." Biochemical Journal 355, no. 1 (February 26, 2001): 51–58. http://dx.doi.org/10.1042/bj3550051.

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In Escherichia coli K-12, c-type cytochromes are synthesized only during anaerobic growth with trimethylamine-N-oxide, nitrite or low concentrations of nitrate as the terminal electron acceptor. A thioredoxin-like protein, CcmG, is one of 12 proteins required for their assembly in the periplasm. Its postulated function is to reduce disulphide bonds formed between correctly paired cysteine residues in the cytochrome c apoproteins prior to haem attachment by CcmF and CcmH. We report that loss of CcmG synthesis by mutation was not compensated by a second mutation in disulphide-bond-forming proteins, DsbA or DsbB, or by the chemical reductant, 2-mercaptoethanesulphonic acid. An anti-CcmG polyclonal antibody was used in Western-blot analysis to probe the redox state of CcmG in mutants defective in the synthesis of other proteins essential for cytochrome c assembly. The oxidized form of CcmG accumulated not only in trxA or dipZ mutants defective in the transfer of electrons from the cytoplasm for disulphide isomerization and reduction reactions in the periplasm, but also in ccmF and ccmH mutants. The requirement of both CcmF and CcmH for the reduction of the disulphide bond in CcmG indicates that CcmG functions later than CcmF and CcmH in cytochrome c assembly, rather than in electron transfer from the membrane-associated DipZ (also known as DsbD) to CcmH. The data support a model proposed by others in which CcmG catalyses one of the last reactions specific to cytochrome c assembly.

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21

Stirnimann, Christian U., Anna Rozhkova, Ulla Grauschopf, Markus G. Grütter, Rudi Glockshuber, and Guido Capitani. "Structural Basis and Kinetics of DsbD-Dependent Cytochrome c Maturation." Structure 13, no. 7 (July 2005): 985–93. http://dx.doi.org/10.1016/j.str.2005.04.014.

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22

Krupp, Rebecca, Cecilia Chan, and Dominique Missiakas. "DsbD-catalyzed Transport of Electrons across the Membrane ofEscherichia coli." Journal of Biological Chemistry 276, no. 5 (November 20, 2000): 3696–701. http://dx.doi.org/10.1074/jbc.m009500200.

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23

Mavridou, Despoina A. I., Julie M. Stevens, Alan D. Goddard, Antony C. Willis, Stuart J. Ferguson, and Christina Redfield. "Control of Periplasmic Interdomain Thiol:Disulfide Exchange in the Transmembrane Oxidoreductase DsbD." Journal of Biological Chemistry 284, no. 5 (November 12, 2008): 3219–26. http://dx.doi.org/10.1074/jbc.m805963200.

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24

Um, Si-Hyeon, Jin-Sik Kim, Kangseok Lee, and Nam-Chul Ha. "Structure of a DsbF homologue fromCorynebacterium diphtheriae." Acta Crystallographica Section F Structural Biology Communications 70, no. 9 (August 29, 2014): 1167–72. http://dx.doi.org/10.1107/s2053230x14016355.

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Disulfide-bond formation, mediated by the Dsb family of proteins, is important in the correct folding of secreted or extracellular proteins in bacteria. In Gram-negative bacteria, disulfide bonds are introduced into the folding proteins in the periplasm by DsbA. DsbE fromEscherichia colihas been implicated in the reduction of disulfide bonds in the maturation of cytochromec. The Gram-positive bacteriumMycobacterium tuberculosisencodes DsbE and its homologue DsbF, the structures of which have been determined. However, the two mycobacterial proteins are able to oxidatively fold a proteinin vitro, unlike DsbE fromE. coli. In this study, the crystal structure of a DsbE or DsbF homologue protein fromCorynebacterium diphtheriaehas been determined, which revealed a thioredoxin-like domain with a typical CXXC active site. Structural comparison withM. tuberculosisDsbF would help in understanding the function of theC. diphtheriaeprotein.

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Rozhkova, Anna, and Rudi Glockshuber. "Kinetics of the Intramolecular Disulfide Exchange Between the Periplasmic Domains of DsbD." Journal of Molecular Biology 367, no. 4 (April 2007): 1162–70. http://dx.doi.org/10.1016/j.jmb.2006.12.033.

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26

Kurokawa, Yoichi, Hideki Yanagi, and Takashi Yura. "Overproduction of Bacterial Protein Disulfide Isomerase (DsbC) and Its Modulator (DsbD) Markedly Enhances Periplasmic Production of Human Nerve Growth Factor inEscherichia coli." Journal of Biological Chemistry 276, no. 17 (January 22, 2001): 14393–99. http://dx.doi.org/10.1074/jbc.m100132200.

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27

Haebel, Peter W., Steven Wichman, David Goldstone, and Peter Metcalf. "Crystallization and Initial Crystallographic Analysis of the Disulfide Bond Isomerase DsbC in Complex with the α Domain of the Electron Transporter DsbD." Journal of Structural Biology 136, no. 2 (November 2001): 162–66. http://dx.doi.org/10.1006/jsbi.2001.4430.

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Cho, Seung-Hyun, Amir Porat, Jiqing Ye, and Jon Beckwith. "Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility." EMBO Journal 26, no. 15 (July 19, 2007): 3509–20. http://dx.doi.org/10.1038/sj.emboj.7601799.

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29

Katzen, F. "Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD." EMBO Journal 21, no. 15 (August 1, 2002): 3960–69. http://dx.doi.org/10.1093/emboj/cdf405.

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30

Andersen, Catherine L., Anne Matthey‐Dupraz, Dominique Missiakas, and Satish Raina. "A new Escherichia coli gene, dsbG , encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins." Molecular Microbiology 26, no. 1 (October 1997): 121–32. http://dx.doi.org/10.1046/j.1365-2958.1997.5581925.x.

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31

Katzen, Federico, and Jon Beckwith. "Transmembrane Electron Transfer by the Membrane Protein DsbD Occurs via a Disulfide Bond Cascade." Cell 103, no. 5 (November 2000): 769–79. http://dx.doi.org/10.1016/s0092-8674(00)00180-x.

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32

Missiakas, D., F. Schwager, and S. Raina. "Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli." EMBO Journal 14, no. 14 (July 1995): 3415–24. http://dx.doi.org/10.1002/j.1460-2075.1995.tb07347.x.

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33

Mavridou, Despoina A. I., Martin Braun, Linda Thöny-Meyer, Julie M. Stevens, and Stuart J. Ferguson. "Avoidance of the cytochrome c biogenesis system by periplasmic CXXCH motifs." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1124–28. http://dx.doi.org/10.1042/bst0361124.

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The CXXCH motif is usually recognized in the bacterial periplasm as a haem attachment site in apocytochromes c. There is evidence that the Escherichia coli Ccm (cytochrome c maturation) system recognizes little more than the CXXCH sequence. A limited number of periplasmic proteins have this motif and yet are not c-type cytochromes. To explore how unwanted haem attachment to CXXCH might be avoided, and to determine whether haem attachment to the surface of a non-cytochrome protein would be possible, we converted the active-site CXXCK motif of a thioredoxin-like protein into CXXCH, the C-terminal domain of the transmembrane oxidoreductase DsbD (cDsbD). The E. coli Ccm system was found to catalyse haem attachment to a very small percentage of the resultant protein (∼0.2%). We argue that cDsbD folds sufficiently rapidly that only a small fraction fails to avoid the Ccm system, in contrast with bona fide c-type cytochromes that only adopt their tertiary structure following haem attachment. We also demonstrate covalent haem attachment at a low level in vivo to the periplasmic disulfide isomerase DsbC, which contains a native CXXCH motif. These observations provide insight into substrate recognition by the Ccm system and expand our understanding of the requirements for covalent haem attachment to proteins. The possible evolutionary relationship between thioredoxins and c-type cytochromes is discussed.

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34

Porat, Amir, Seung-Hyun Cho, and Jon Beckwith. "The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases." Research in Microbiology 155, no. 8 (October 2004): 617–22. http://dx.doi.org/10.1016/j.resmic.2004.05.005.

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35

Rozhkova, Anna, Christian U. Stirnimann, Patrick Frei, Ulla Grauschopf, René Brunisholz, Markus G. Grütter, Guido Capitani, and Rudi Glockshuber. "Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD." EMBO Journal 23, no. 8 (April 1, 2004): 1709–19. http://dx.doi.org/10.1038/sj.emboj.7600178.

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36

Smith, Roxanne P., Biswaranjan Mohanty, Martin L. Williams, Martin J. Scanlon, and Begoña Heras. "HN, N, Cα and Cβ assignments of the two periplasmic domains of Neisseria meningitidis DsbD." Biomolecular NMR Assignments 11, no. 2 (June 6, 2017): 181–86. http://dx.doi.org/10.1007/s12104-017-9743-x.

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37

Tan, Jacqueline, Ying Lu, and James C. A. Bardwell. "Mutational Analysis of the Disulfide Catalysts DsbA and DsbB." Journal of Bacteriology 187, no. 4 (February 15, 2005): 1504–10. http://dx.doi.org/10.1128/jb.187.4.1504-1510.2005.

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ABSTRACT In prokaryotes, disulfides are generated by the DsbA-DsbB system. DsbB functions to generate disulfides by quinone reduction. These disulfides are passed to the DsbA protein and then to folding proteins. To investigate the DsbA-DsbB catalytic system, we performed an in vivo selection for chromosomal dsbA and dsbB mutants. We rediscovered many residues previously shown to be important for the activity of these proteins. In addition, we obtained one novel DsbA mutant (M153R) and four novel DsbB mutants (L43P, H91Y, R133C, and L146R). We also mutated residues that are highly conserved within the DsbB family in an effort to identify residues important for DsbB function. We found classes of mutants that specifically affect the apparent Km of DsbB for either DsbA or quinones, suggesting that quinone and DsbA may interact with different regions of the DsbB protein. Our results are consistent with the interpretation that the residues Q33 and Y46 of DsbB interact with DsbA, Q95 and R48 interact with quinones, and that residue M153 of DsbA interacts with DsbB. All of these interactions could be due to direct amino acid interactions or could be indirect through, for instance, their effect on protein structure. In addition, we find that the DsbB H91Y mutant severely affects the k cat of the reaction between DsbA and DsbB and that the DsbB L43P mutant is inactive, suggesting that both L43 and H91 are important for the activity of DsbB. These experiments help to better define the residues important for the function of these two protein-folding catalysts.

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38

Goulding, Celia W., Michael R. Sawaya, Angineh Parseghian, Vincent Lim, David Eisenberg, and Dominique Missiakas. "Thiol−Disulfide Exchange in an Immunoglobulin-like Fold: Structure of the N-Terminal Domain of DsbD†,‡." Biochemistry 41, no. 22 (June 2002): 6920–27. http://dx.doi.org/10.1021/bi016038l.

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39

Hemmis, Casey, Mehmet Berkmen, Markus Eser, and Joel Schildbach. "TrbB from Conjugative Plasmid F: A Representative of a New Class of Dsbd-Dependent Disulfide Isomerases." Biophysical Journal 100, no. 3 (February 2011): 193a. http://dx.doi.org/10.1016/j.bpj.2010.12.1271.

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40

Stevens, Julie M., Euan H. Gordon, and Stuart J. Ferguson. "Overproduction of CcmABCDEFGH restores cytochromecmaturation in a DsbD deletion strain ofE. coli: another route for reductant?" FEBS Letters 576, no. 1-2 (September 11, 2004): 81–85. http://dx.doi.org/10.1016/j.febslet.2004.08.067.

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41

Stelzl, Lukas S., Despoina A. I. Mavridou, Stuart J. Ferguson, Andrew J. Baldwin, Mark S. P. Sansom, and Christina Redfield. "Studying the Conformational Equilibrium of the N-Terminal Domain of Dsbd by NMR and Computer Simulation." Biophysical Journal 108, no. 2 (January 2015): 184a. http://dx.doi.org/10.1016/j.bpj.2014.11.1017.

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42

Mavridou, Despoina A. I., Julie M. Stevens, Stuart J. Ferguson, and Christina Redfield. "Active-site Properties of the Oxidized and Reduced C-terminal Domain of DsbD Obtained by NMR Spectroscopy." Journal of Molecular Biology 370, no. 4 (July 2007): 643–58. http://dx.doi.org/10.1016/j.jmb.2007.04.038.

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43

Raczko, Anna M., Janusz M. Bujnicki, Marcin Pawłowski, Renata Godlewska, Magdalena Lewandowska, and Elżbieta K. Jagusztyn-Krynicka. "Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria." Microbiology 151, no. 1 (January 1, 2005): 219–31. http://dx.doi.org/10.1099/mic.0.27483-0.

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In Gram-negative bacterial cells, disulfide bond formation occurs in the oxidative environment of the periplasm and is catalysed by Dsb (disulfide bond) proteins found in the periplasm and in the inner membrane. In this report the identification of a new subfamily of disulfide oxidoreductases encoded by a gene denoted dsbI, and functional characterization of DsbI proteins from Campylobacter jejuni and Helicobacter pylori, as well as DsbB from C. jejuni, are described. The N-terminal domain of DsbI is related to DsbB proteins and comprises five predicted transmembrane segments, while the C-terminal domain is predicted to locate to the periplasm and to fold into a β-propeller structure. The dsbI gene is co-transcribed with a small ORF designated dba ( dsbI-accessory). Based on a series of deletion and complementation experiments it is proposed that DsbB can complement the lack of DsbI but not the converse. In the presence of DsbB, the activity of DsbI was undetectable, hence it probably acts only on a subset of possible substrates of DsbB. To reconstruct the principal events in the evolution of DsbB and DsbI proteins, sequences of all their homologues identifiable in databases were analysed. In the course of this study, previously undetected variations on the common thiol-oxidoreductase theme were identified, such as development of an additional transmembrane helix and loss or migration of the second pair of Cys residues between two distinct periplasmic loops. In conjunction with the experimental characterization of two members of the DsbI lineage, this analysis has resulted in the first comprehensive classification of the DsbB/DsbI family based on structural, functional and evolutionary criteria.

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44

Kadokura, Hiroshi, Lorenzo Nichols, and Jon Beckwith. "Mutational Alterations of the Key cis Proline Residue That Cause Accumulation of Enzymatic Reaction Intermediates of DsbA, a Member of the Thioredoxin Superfamily." Journal of Bacteriology 187, no. 4 (February 15, 2005): 1519–22. http://dx.doi.org/10.1128/jb.187.4.1519-1522.2005.

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ABSTRACT The DsbA-DsbB pathway introduces disulfide bonds into newly translocated proteins. Conversion of the conserved cis proline 151 of DsbA to several hydrophilic residues results in accumulation of mixed disulfides between DsbA and its dedicated oxidant, DsbB. However, only a proline-to-threonine change causes accumulation of mixed disulfides of DsbA with its substrates.

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45

Hemmis, C. W., M. Berkmen, M. Eser, and J. F. Schildbach. "TrbB from Conjugative Plasmid F Is a Structurally Distinct Disulfide Isomerase That Requires DsbD for Redox State Maintenance." Journal of Bacteriology 193, no. 18 (July 8, 2011): 4588–97. http://dx.doi.org/10.1128/jb.00351-11.

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46

Sardesai, Abhijit A., and J. Gowrishankar. "trans-Acting Mutations in Loci Other than kdpDE That Affect kdp Operon Regulation inEscherichia coli: Effects of Cytoplasmic Thiol Oxidation Status and Nucleoid Protein H-NS on kdpExpression." Journal of Bacteriology 183, no. 1 (January 1, 2001): 86–93. http://dx.doi.org/10.1128/jb.183.1.86-93.2001.

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ABSTRACT Transcription of the K+ transport operonkdp in Escherichia coli is induced during K+-limited growth by the action of a dual-component phosphorelay regulatory system comprised of a sensor kinase (integral membrane protein), KdpD, and a DNA-binding response regulator (cytoplasmic protein), KdpE. In this study, we screened for newdke (named dke for decreased kdpexpression) mutations (in loci other than kdpDE) that led to substantially decreased kdp expression. Onedke mutation was shown to be in hns, encoding the nucleoid protein H-NS. Another dke mutation was mapped to trxB (encoding thioredoxin reductase), and an equivalent reduction in kdp expression was demonstrated also fortrxA mutants that are deficient in thioredoxin 1. Exogenously provided dithiothreitol rescued the kdpexpression defect in trxB but not trxA mutants. Neither trxB nor trxA affected gene regulation mediated by another dual-component system tested, EnvZ-OmpR. Mutations in genes dsbC and dsbD did not affectkdp expression, suggesting that the trx effects on kdp are not mediated by alterations in protein disulfide bond status in the periplasm. Reduced kdp expression was observed even in a trxB strain that harbored a variant KdpD polypeptide bearing no Cys residues. A trxB hns double mutant was even more severely affected for kdp expression than either single mutant. The dke mutations themselves had no effect on strength of the signal controlling kdpexpression, and constitutive mutations in kdpDE were epistatic to hns and trxB. These results indicate that perturbations in cytoplasmic thiol oxidation status and in levels of the H-NS protein exert additive effects, direct or indirect, at a step(s) upstream of KdpD in the signal transduction pathway, which significantly influence the magnitude of KdpD kinase activity obtained for a given strength of the inducing signal forkdp transcription.

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47

Totsika, Makrina, Begoña Heras, Daniël J. Wurpel, and Mark A. Schembri. "Characterization of Two Homologous Disulfide Bond Systems Involved in Virulence Factor Biogenesis in Uropathogenic Escherichia coli CFT073." Journal of Bacteriology 191, no. 12 (April 17, 2009): 3901–8. http://dx.doi.org/10.1128/jb.00143-09.

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ABSTRACT Disulfide bond (DSB) formation is catalyzed by disulfide bond proteins and is critical for the proper folding and functioning of secreted and membrane-associated bacterial proteins. Uropathogenic Escherichia coli (UPEC) strains possess two paralogous disulfide bond systems: the well-characterized DsbAB system and the recently described DsbLI system. In the DsbAB system, the highly oxidizing DsbA protein introduces disulfide bonds into unfolded polypeptides by donating its redox-active disulfide and is in turn reoxidized by DsbB. DsbA has broad substrate specificity and reacts readily with reduced unfolded proteins entering the periplasm. The DsbLI system also comprises a functional redox pair; however, DsbL catalyzes the specific oxidative folding of the large periplasmic enzyme arylsulfate sulfotransferase (ASST). In this study, we characterized the DsbLI system of the prototypic UPEC strain CFT073 and examined the contributions of the DsbAB and DsbLI systems to the production of functional flagella as well as type 1 and P fimbriae. The DsbLI system was able to catalyze disulfide bond formation in several well-defined DsbA targets when provided in trans on a multicopy plasmid. In a mouse urinary tract infection model, the isogenic dsbAB deletion mutant of CFT073 was severely attenuated, while deletion of dsbLI or assT did not affect colonization.

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48

Quinternet, Marc, Pascale Tsan, Laure Selme-Roussel, Christophe Jacob, Sandrine Boschi-Muller, Guy Branlant, and Manh-Thong Cung. "Formation of the Complex between DsbD and PilB N-Terminal Domains from Neisseria meningitidis Necessitates an Adaptability of nDsbD." Structure 17, no. 7 (July 2009): 1024–33. http://dx.doi.org/10.1016/j.str.2009.05.011.

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49

Katzen, F., and J. Beckwith. "Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD." Proceedings of the National Academy of Sciences 100, no. 18 (August 18, 2003): 10471–76. http://dx.doi.org/10.1073/pnas.1334136100.

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50

Bessette, Paul H., Ji Qiu, James C. A. Bardwell, James R. Swartz, and George Georgiou. "Effect of Sequences of the Active-Site Dipeptides of DsbA and DsbC on In Vivo Folding of Multidisulfide Proteins inEscherichia coli." Journal of Bacteriology 183, no. 3 (February 1, 2001): 980–88. http://dx.doi.org/10.1128/jb.183.3.980-988.2001.

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ABSTRACT We have examined the role of the active-site CXXC central dipeptides of DsbA and DsbC in disulfide bond formation and isomerization in the Escherichia coli periplasm. DsbA active-site mutants with a wide range of redox potentials were expressed either from the trc promoter on a multicopy plasmid or from the endogenous dsbA promoter by integration of the respective alleles into the bacterial chromosome. ThedsbA alleles gave significant differences in the yield of active murine urokinase, a protein containing 12 disulfides, including some that significantly enhanced urokinase expression over that allowed by wild-type DsbA. No direct correlation between the in vitro redox potential of dsbA variants and the urokinase yield was observed. These results suggest that the active-site CXXC motif of DsbA can play an important role in determining the folding of multidisulfide proteins, in a way that is independent from DsbA's redox potential. However, under aerobic conditions, there was no significant difference among the DsbA mutants with respect to phenotypes depending on the oxidation of proteins with few disulfide bonds. The effect of active-site mutations in the CXXC motif of DsbC on disulfide isomerization in vivo was also examined. A library of DsbC expression plasmids with the active-site dipeptide randomized was screened for mutants that have increased disulfide isomerization activity. A number of DsbC mutants that showed enhanced expression of a variant of human tissue plasminogen activator as well as mouse urokinase were obtained. These DsbC mutants overwhelmingly contained an aromatic residue at the C-terminal position of the dipeptide, whereas the N-terminal residue was more diverse. Collectively, these data indicate that the active sites of the soluble thiol- disulfide oxidoreductases can be modulated to enhance disulfide isomerization and protein folding in the bacterial periplasmic space.

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