The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase

Biochemical and Biophysical Research Communications

Volumn 343, Issue 3, 2006, Pages 780-786

  Caldas, Thérèse ^a   Malki, Abderrahim ^a   Kern, Renée ^a   Abdallah, Jad ^a   Richarme, Gilbert ^a  

^a INSTITUT JACQUES MONOD   (France)

Author keywords

Chaperone; Heat shock; Oxidoreductase; SxxC; YbbN

Indexed keywords

BACTERIAL TOXIN; CHAPERONE; CYSTEINE; OLIGOMER; OXIDOREDUCTASE; RIBONUCLEASE; SERINE; TETRAMER; THIOREDOXIN; UREA;

ARTICLE; CATALYSIS; CELL FUNCTION; DENATURATION; ESCHERICHIA COLI; HEAT SHOCK; IN VIVO STUDY; ISOMERIZATION; NONHUMAN; OXIDATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; CYSTEINE; DISULFIDES; ESCHERICHIA COLI PROTEINS; INSULIN; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; OXIDOREDUCTASES ACTING ON SULFUR GROUP DONORS; PROTEIN FOLDING; RIBONUCLEASES; THIOREDOXIN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 33645951646     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.03.028     Document Type: Article

References (38)

1. Arner E.S., and Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 26 (2000) 6102-6109
2. Miranda-Vizuete A., Damdidopoulos A.E., Gustafsson J., and Spyrou G. Cloning, overexpression, and characterization of a novel Escherichia coli thioredoxin. J. Biol. Chem. 272 (1997) 30837-30841
3. Ritz D., Patel H., Doan B., Zheng M., Aslund F., Storz G., and Beckwith J. Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli. J. Biol. Chem. 275 (2000) 2505-2512
4. Holmgren A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264 (1989) 13963-13966
5. Gilbert H.F. Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. Relat. Areas Mol. Biol. 63 (1990) 69-172
6. Derman A.I., Prinz W.A., Belin D., and Beckwith J. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262 (1993) 1744-1747
7. Debarbieux L., and Beckwith J. Electron avenue: pathways of disulfide bond formation and isomerization. Cell 99 (1999) 117-119
8. Prinz W.A., Aslund F., Holmgren A., and Beckwith J. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J. Biol. Chem. 272 (1997) 15661-15667
9. Collet J.F., D'Souza J.C., Jakob U., and Bardwell J.C. Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. J. Biol. Chem. 278 (2003) 45325-45332
10. Fomenko D.E., and Gladyshev V.N. Identity and functions of CxxC-derived motifs. Biochemistry 42 (2003) 11214-11225
11. Pigiet V.P., and Schuster B.J. Thioredoxin-catalyzed refolding of disulfide-containing proteins. Proc. Natl. Acad. Sci. USA 83 (1986) 7643-7647
12. de Crouy-Chanel A., Kohiyama M., and Richarme G. A novel function of Escherichia coli chaperone DnaJ. J. Biol. Chem. 270 (1995) 22669-22672
13. Jakob U., Gaestel M., Engel K., and Buchner J. Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268 (1993) 1517-1520
14. Richarme G., and Caldas T.D. Chaperone properties of the bacterial periplasmic substrate-binding proteins. J. Biol. Chem. 272 (1997) 15607-15612
15. Eklund H., Gleason F.K., and Holmgren A. Structural and functional relations among thioredoxins of different species. Proteins 11 (1991) 13-28
16. Dyson H.J., Gippert G.P., Case D.A., Holmgren A., and Wright P.E. Three-dimensional structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy. Biochemistry 29 (1990) 4129-4136
17. Forman-Kay J.D., Clore G.M., Wingfield P.T., and Gronenborn A.M. 1H and 15N resonance assignments and secondary structure of the human thioredoxin C62A, C69A, C73A mutant. Biochemistry 30 (1991) 2685-2698
18. Hawkins H.C., Balckburn E.C., and Freedman R.B. Comparison of the activities of protein disulphide isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate. Biochem. J. 275 (1991) 349-353
19. Careaga C.L., and Falke J.J. Thermal motions of surface alpha-helices in the d galactose chemosensory receptor. Detection by disulfide trapping. J. Mol. Biol. 226 (1992) 1219-1235
20. Chivers P.T., and Raines R.T. General acid/base catalysis in the active site of Escherichia coli thioredoxin. Biochemistry 36 (1997) 15810-15815
21. Schönfeld H.J., Schmidt D., Schroder H., and Bukau B. The DnaK chaperone system of Escherichia coli: quartenary structures and interactions of the DnaK and GrpE components. J. Biol. Chem. 270 (1995) 2183-2189
22. Russel M., and Model P. The role of thioredoxin in filamentous phage assembly. Construction, isolation and characterization of mutant thioredoxins. J. Biol. Chem. 261 (1986) 14997-15004
23. Akiyama Y., Kamitani S., Kusukawa N., and Ito K. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA gene product. J. Biol. Chem. 267 (1992) 22440-22445
24. Bardwell J.C.A., McGovern K., and Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell 67 (1991) 581-589
25. Vlamis-Gardikas A., Aslund F., Spyrou G., Bergman T., and Holmgren A. Cloning, overexpression, and characterization of glutaredoxin 2, an atypical thioredoxin from Escherichia coli. J. Biol. Chem. 272 (1997) 11236-11243
26. Shao F., Bader M.W., Jakob U., and Bardwell J.C. DsbG, a protein disulfide isomerase with chaperone activity. J. Biol. Chem. 275 (2000) 13349-13352
27. Tsai B., Rodighiero C., Lencer W.I., and Rapoport T.A. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104 (2001) 937-948
28. Hartl F.U., and Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chains to folded proteins. Science 195 (2002) 1852-1858
29. Kern R., Malki A., Holmgren A., and Richarme G. Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase. Biochem. J. 371 (2003) 965-972
30. Dougan D.A., Mogk A., and Bukau B. Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question. Cell Mol. Life Sci. 59 (2002) 1607-1616
31. Buchner J., Schmidt M., Fuchs M., Jaenicke R., Rudolph R., Schmid F.X., and Kiefhaber T. GroE facilitates refolding of citrate synthase by suppressing its aggregation. Biochemistry 30 (1991) 1586-1591
32. Liberek K., Skowyra D., Zylicz M., Johnson C., and Georgopoulos C. The DnaK chaperone changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein. J. Biol. Chem. 266 (1991) 14491-14496
33. Capitani G., Markovic-Housley Z., DelVal G., Morris M., Jansonius J.N., and Schürmann P. Crystal structure of two functionally different thioredoxins in spinach chloroplasts. J. Mol. Biol. 302 (2000) 135-154
34. Geck M.K., Larimer F.W., and Hartman F.C. The molecular pathway for the regulation of phosphoribulokinase by thioredoxin f. J. Biol. Chem. 271 (1996) 24736-24740
35. Andersen J.F., Sanders D.A.R., Gasdaska J.R., Weichsel A., Powis G., and Montfort W.R. Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60-arginine mutant. Biochemistry 36 (1997) 13979-13988
36. Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss Pdb viewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
37. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTALW: Improving the sensitivity of progressive multiple sequence alignements through sequence weighting, positions specific gap penalties and weight matrix choice. Nucleic Acid Res. 22 (1994) 4673-4680
38. Perriere G., Duret L., and Gouy M. HOBACGEN: Database system for comparative genomics in bacteria. Genome Res. 10 (2000) 379-385