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Disulfide bond formation in the Escherichia coli cytoplasm: an invivo role reversal for the thioredoxins
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- Åberg A, Hahne S, Karlsson M, Larsson A, Ormü M, Åhgren A and Sjüberg BM (1989) Evidence for two different classes of redox‐active cysteines in ribonucleotide reductase of Escherichia coli. J Biol Chem, 264, 12249‐12252. · DOI
- Åslund F, Ehn B, Miranda‐Vizuete A, Pueyo C and Holmgren A (1994) Two additional glutaredoxins exist in Escherichia coli: Glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant. Proc Natl Acad Sci USA, 91, 9813‐9817. · DOI
- Åslund F, Berndt KD and Holmgren A (1997) Redox potentials of glutaredoxins and other thiol‐disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein‐protein redox equilibria. J Biol Chem, 272, 30780‐30786. · DOI · Paper page
- Bardwell JCA, McGovern K and Beckwith J (1991) Identification of a protein required for disulfide bond formation in vivo. Cell, 67, 581‐589. · DOI
- Boyd D, Manoil C and Beckwith J (1987) Determinants of membrane protein topology. Proc Natl Acad Sci USA, 84, 8525‐8529. · DOI · Paper page
- Creighton TE and Goldenberg DP (1984) Kinetic role of a meta‐stable native‐like two‐disulphide species in the folding transition of bovine pancreatic trypsin inhibitor. J Mol Biol, 179, 497‐526. · DOI
- Debarbieux L and Beckwith J (1998) The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm. Proc Natl Acad Sci USA, 95, 10751‐10756. · DOI
- Derman AI and Beckwith J (1991) Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm. J Bacteriol, 173, 7719‐7722. · DOI
- Derman AI, Prinz WA, Belin D and Beckwith J (1993a) Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science, 262, 1744‐1747. · DOI
- Derman AI, Puziss JW, Bassford PJ,Jr and Beckwith J (1993b) A signal sequence is not required for protein export in prlA mutants of Escherichia coli. EMBO J, 12, 879‐888. · DOI
- Fraser CM et al. (1995) The minimal gene complement of Mycoplasma genitalium. Science, 270, 397‐403. · DOI · Paper page
- Gil D and Bouché JP (1991) ColE1‐type vectors with fully repressible replication. Gene, 105, 17‐22. · DOI
- Guzman L‐M, Belin D, Carson MJ and Beckwith J (1995) Tight regulation, modulation and high‐level expression by vectors containing the arabinose pBAD promoter. J Bacteriol, 177, 4121‐4130. · DOI · Paper page
- Gvakharia BO, Hanson E, Koonin EK and Mathewes CK (1996) Identification of a second functional glutaredoxin encoded by the bacteriophage T4 genome. J Biol Chem, 271, 15307‐15310. · DOI
- Himmelreich R, Hilbert H, Plagens H, Pirkl E, Li BC and Herrmann R (1996) Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae. Nucleic Acids Res, 24, 4420‐4449. · DOI · Paper page
- Holmgren A (1989) Thioredoxin and glutaredoxin systems. J Biol Chem, 264, 13963‐13966. · DOI
- Jordan A, Åslund F, Pontis E, Reichard P and Holmgren A (1997) Characterization of Escherichia coli NrdH: A glutaredoxin‐like protein with a thioredoxin‐like activity profile. J Biol Chem, 272, 18044‐18050. · DOI
- Lim CJ, Sa JH and Fuchs JA (1996) Identification of a third thioredoxin gene from Corynebacterium nephridii. Biochim Biophys Acta, 1307, 13‐16. · DOI
- Link AJ, Phillips D and Church GM (1997) Methods for generating precise deletions and insertions in the genome of wild‐type Escherichia coli: application to open reading frame characterization. J Bacteriol, 179, 6228‐6237. · DOI · Paper page
- Liu J and Rosen BP (1997) Ligand interactions of the ArsC arsenate reductase. J Biol Chem, 272, 21084‐21089. · DOI
- Lundstrüm J, Krause G and Holmgren A (1992) A Pro to His mutation in active site of thioredoxin increases its disulfide‐isomerase activity 10‐fold. New refolding systems for reduced or randomly oxidized ribonuclease. J Biol Chem, 267, 9047‐9052. · DOI
- Michaelis S, Hunt J and Beckwith J (1986) Effects of signal sequence mutations on the kinetics of alkaline phosphatase export to the periplasm in Escherichia coli. J Bacteriol, 167, 160‐167. · DOI
- Miranda‐Vizuete A, Damdimopoulos AE, Gustafsson J‐A and Spyrou G (1997) Cloning, expression and characterization of a novel Escherichia coli thioredoxin. J Biol Chem, 272, 30841‐30847. · DOI
- Missiakas D, Schwager F and Raina S (1995) Identification and characterization of a new disulfide isomerase‐like protein (DsbD) in Escherichia coli. EMBO J, 14, 3415‐3424. · DOI
- Mulliez E, Ollagnier S, Fontecave M, Eliasson R and Reichard P (1995) Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli. Proc Natl Acad Sci USA, 92, 8759‐8762. · DOI
- Pigiet V and Schuster BJ (1986) Thioredoxin‐catalyzed refolding of disulfide‐containing proteins. Proc Natl Acad Sci USA, 83, 7643‐7647. · DOI
- Pogliano KJ and Beckwith J (1993) The Cs sec mutants of Escherichia coli reflect the cold sensitivity of protein export itself. Genetics, 133, 763‐773. · DOI
- Pollitt S and Zalkin H (1983) Role of primary structure and disulfide bond formation in β‐lactamase secretion. J Bacteriol, 153, 27‐32. · DOI
- Prinz WA, Åslund F, Holmgren A and Beckwith J (1997) The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J Biol Chem, 272, 15661‐15667. · DOI
- Ren X, Bjürnstedt M, Shen B, Ericson ML and Holmgren A (1993) Mutagenesis of structural half‐cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione. Biochemistry, 32, 9701‐9708. · DOI
- Rietsch A and Beckwith J (1998) The genetics of disulfide bond metabolism. Annu Rev Genet, 32, 163‐184. · DOI
- Rietsch A, Belin D, Martin N and Beckwith J (1996) An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc Natl Acad Sci USA, 93, 13048‐13053. · DOI · Paper page
- Rivera‐Madrid R, Mestres D, Marinho P, Jacquot J‐P, Decottignies P, Miginiac‐Maslow M and Meyer Y (1995) Evidence for five divergent thioredoxin h sequences in Arabidopsis thaliana. Proc Natl Acad Sci USA, 92, 5620‐5624. · DOI
- Russel M and Model P (1986) The role of thioredoxin in filamentous phage assembly. Construction, isolation and characterization of mutant thioredoxins. J Biol Chem, 261, 14997‐15005. · DOI
- Russel M, Model P and Holmgren A (1990) Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis. J Bacteriol, 172, 1923‐1929. · DOI
- Singer M et al. (1989) A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli. Microbiol Rev, 53, 1‐24. · DOI
- Sone M, Kishigami S, Yoshihisa T and Ito K (1997) Roles of disulfide bonds in bacterial alkaline phosphatase. J Biol Chem, 272, 6174‐6178. · DOI
- Wetterauer B, Jacquot JP and Veron M (1992) Thioredoxins from Dictyostelium discoideum are a developmentally regulated multigene family. J Biol Chem, 267, 9895‐9904. · DOI
- Zheng M, Åslund F and Storz G (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation. Science, 279, 1718‐1721. · DOI · Paper page
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Metadata
- Authors
- Stewart, E. J.
- Venue
- The EMBO Journal
- Published
- 1998-10-01
- Volume
- 17
- Issue
- 19
- Pages
- 5543-5550
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W2156366212
- Cited by
- 432
- References
- 0
- FWCI
- 5.06
- Type
- journal article
- Language
- en
- Open access
- green
- Licence
- www.springer.com/tdm (tdm)
- www.springer.com/tdm (vor)
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