Mutant AhpC Peroxiredoxins Suppress Thiol-Disulfide Redox Deficiencies and Acquire Deglutathionylating Activity

Molecular Cell

Volumn 29, Issue 1, 2008, Pages 36-45

  Yamamoto, Yuji ^a   Ritz, Dani ^b   Planson, Anne Gaëlle ^b   Jönsson, Thomas J ^a   Faulkner, Melinda J ^b   Boyd, Dana ^b   Beckwith, Jon ^b   Poole, Leslie B ^a  

^a WAKE FOREST SCHOOL OF MEDICINE   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

PROTEINS

Indexed keywords

CYSTEINE; DISULFIDE; GLUTAREDOXIN; GLUTATHIONE; PEROXIDASE; PEROXIREDOXIN; PEROXIREDOXIN AHPC; THIOL; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVITY; ENZYME MECHANISM; IN VITRO STUDY; IN VIVO STUDY; POINT MUTATION; PROTEIN FUNCTION;

AMINO ACID SUBSTITUTION; CYSTEINE; DIMERIZATION; DISULFIDES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLUTAREDOXINS; GLUTATHIONE; HYDROGEN PEROXIDE; MODELS, MOLECULAR; MUTAGENESIS, INSERTIONAL; OXIDATION-REDUCTION; OXIDATIVE STRESS; OXIDOREDUCTASES; PEROXIREDOXINS; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN SUBUNITS; SUBSTRATE SPECIFICITY; TRINUCLEOTIDE REPEATS;

BACTERIA (MICROORGANISMS);

EID: 38149008764     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2007.11.029     Document Type: Article

References (20)

1. Åslund F., and Beckwith J. Bridge over troubled waters: sensing stress by disulfide bond formation. Cell 96 (1999) 751-753
2. Christman M.F., Morgan R.W., Jacobson F.S., and Ames B.N. Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell 41 (1985) 753-762
3. Christman M.F., Storz G., and Ames B.N. OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins. Proc. Natl. Acad. Sci. USA 86 (1989) 3484-3488
4. Derman A.I., and Beckwith J. Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: a caution for gene fusion studies. J. Bacteriol. 177 (1995) 3764-3770
5. Ellis H.R., and Poole L.B. Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium. Biochemistry 36 (1997) 13349-13356
6. Fernandes A.P., Fladvad M., Berndt C., Andresen C., Lillig C.H., Neubauer P., Sunnerhagen M., Holmgren A., and Vlamis-Gardikas A. A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase. J. Biol. Chem. 280 (2005) 24544-24552
7. Hofmann B., Hecht H.-J., and Flohé L. Peroxiredoxins. Biol. Chem. 383 (2002) 347-364
8. Jönsson T.J., Ellis H.R., and Poole L.B. Cysteine reactivity and thiol-disulfide interchange pathways in AhpF and AhpC of the bacterial alkyl hydroperoxide reductase system. Biochemistry 46 (2007) 5709-5721
9. Koo K.H., Lee S., Jeong S.Y., Kim E.T., Kim H.J., Song K., and Chae H.-Z. Regulation of thioredoxin peroxidase activity by C-terminal truncation. Arch. Biochem. Biophys. 397 (2002) 312-318
10. Liochev S.I., and Fridovich I. Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Proc. Natl. Acad. Sci. USA 89 (1992) 5892-5896
11. Masip L., Veeravalli K., and Georgiou G. The many faces of glutathione in bacteria. Antioxid. Redox Signal. 8 (2006) 753-762
12. Miller J.H. Experiments in Molecular Genetics (1972), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
13. Ortenberg R., Gon S., Porat A., and Beckwith J. Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli. Proc. Natl. Acad. Sci. USA 101 (2004) 7439-7444
14. Parsonage D., Youngblood D.S., Sarma G.N., Wood Z.A., Karplus P.A., and Poole L.B. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry 44 (2005) 10583-10592
15. Poole L.B. Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases. Arch. Biochem. Biophys. 433 (2005) 240-254
16. Porras P., Pedrajas J.R., Martinez-Galisteo E., Padilla C.A., Johansson C., Holmgren A., and Barcena J.A. Glutaredoxins catalyze the reduction of glutathione by dihydrolipoamide with high efficiency. Biochem. Biophys. Res. Commun. 295 (2002) 1046-1051
17. 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
18. Ritz D., Lim J., Reynolds C.M., Poole L.B., and Beckwith J. Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion. Science 294 (2001) 158-160
19. Wood Z.A., Poole L.B., Hantgan R.R., and Karplus P.A. Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins. Biochemistry 41 (2002) 5493-5504
20. Wood Z.A., Poole L.B., and Karplus P.A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300 (2003) 650-653