Identification of a redox-regulated chaperone network

EMBO Journal

Volumn 23, Issue 1, 2004, Pages 160-168

  Hoffmann, Jörg H ^a   Linke, Katrin ^a   Graf, Paul C F ^a   Lilie, Hauke ^b   Jakob, Ursula ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

Chaperone; Disulfide bond; Hsp33; Oxidative stress; Redox regulation

Indexed keywords

CHAPERONE; CHAPERONIN; GLUCOSE REGULATED PROTEIN; GLUTAREDOXIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 33; PROTEIN DNAJ; PROTEIN DNAK; THIOREDOXIN; UNCLASSIFIED DRUG;

ARTICLE; DIMERIZATION; DISULFIDE BOND; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING;

ANIMALS; CATTLE; CITRATE (SI)-SYNTHASE; CYSTEINE; DIMERIZATION; DISULFIDES; DITHIOTHREITOL; FLUORESCENCE POLARIZATION; HEAT-SHOCK PROTEINS; LUCIFERASES; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; REDUCING AGENTS; SERUM ALBUMIN, BOVINE; SUBSTRATE SPECIFICITY; SWINE; TEMPERATURE; TIME FACTORS;

EID: 0842328576     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600016     Document Type: Article

References (20)

1. Aslund F, Zheng M, Beckwith J, Storz G (1999) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc Natl Acad Sci USA 96: 6161-6165
2. Barbirz S, Jakob U, Glocker MO (2000) Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone. J Biol Chem 275: 18759-18766
3. Beissinger M, Buchner J (1998) How chaperones fold proteins. Biol Chem 379: 245-259
4. Buchberger A, Schroder H, Buttner M, Valencia A, Bukau B (1994) A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nat Struct Biol 1: 95-101
5. Buchner J, Schmidt M, Fuchs M, Jaenicke R, Rudolph R, Schmid FX, Kiefhaber T (1991) GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry 30: 1586-1591
6. Crouy-Chanel A, Kohiyama M, Richarme G (1999) Interaction of DnaK with native proteins and membrane proteins correlates with their accessible hydrophobicity. Gene 230: 163-170
7. Deuerling E, Patzelt H, Vorderwulbecke S, Rauch T, Kramer G, Schaffitzel E, Mogk A, Schulze-Specking A, Langen H, Bukau B (2003) Trigger factor and DnaK possess overlapping substrate pools and binding specificities. Mol Microbiol 47: 1317-1328
8. Echave P, Esparza-Ceron MA, Cabiscol E, Tamarit J, Ros J, Membrillo-Hernandez J, Lin EC (2002) DnaK dependence of mutant ethanol oxidoreductases evolved for aerobic function and protective role of the chaperone against protein oxidative damage in Escherichia coli. Proc Natl Acad Sci USA 99: 4626-4631
9. Ellis RJ, van der Vies SM, Hemmingsen SM (1989) The molecular chaperone concept. Biochem Soc Symp 55: 145-153
10. Graumann J, Lilie H, Tang X, Tucker KA, Hoffmann JH, Vijayalakshmi J, Saper M, Bardwell JC, Jakob U (2001) Activation of the redox-regulated molecular chaperone Hsp33-a two-step mechanism. Structure (Camb) 9: 377-387
11. Herbst R, Schafer U, Seckler R (1997) Equilibrium intermediates in the reversible unfolding of firefly (Photinus pyralis) luciferase. J Biol Chem 272: 7099-7105
12. Jakob U, Eser M, Bardwell JC (2000) Redox switch of hsp33 has a novel zinc-binding motif. J Biol Chem 275: 38302-38310
13. Jakob U, Muse W, Eser M, Bardwell JC (1999) Chaperone activity with a redox switch. Cell 96: 341-352
14. Mogk A, Schlieker C, Friedrich KL, Schonfeld HJ, Vierling E, Bukau B (2003) Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J Biol Chem 278: 31033-31042
15. Mogk A, Tomoyasu T, Goloubinoff P, Rudiger S, Roder D, Langen H, Bukau B (1999) Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. Embo J 18: 6934-6949
16. Prinz WA, Aslund F, Holmgren A, 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
17. Straus D, Walter W, Gross CA (1990) DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32. Genes Dev 4: 2202-2209
18. Tsai B, Rodighiero C, Lencer WI, Rapoport TA (2001) Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104: 937-948
19. Veinger L, Diamant S, Buchner J, Goloubinoff P (1998) The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J Biol Chem 273: 11032-11037
20. Zheng M, Aslund F, Storz G (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279: 1718-1721