The putative thiol-disulphide interchange protein DsbG from Acidithiobacillus ferrooxidans has disulphide isomerase activity

ScienceAsia

Volumn 36, Issue 2, 2010, Pages 100-104

  Zhang, Cheng Gui ^a,b   Xia, Jin Ian ^a   Liu, Yuan Dong ^a   He, Huan ^a   Qiu, Guan Zhou ^a  

^a CENTRAL SOUTH UNIVERSITY   (China)

^b DALI UNIVERSITY   (China)

Author keywords

Disulphide isomerization activity; Site directed mutagenesis; Thiol disulphide interchange protein

Indexed keywords

EID: 77954927666     PISSN: 15131874     EISSN: None     Source Type: Journal    
DOI: 10.2306/scienceasia1513-1874.2010.36.100     Document Type: Article

References (14)

1. Raina S, Missiakas D (1997) Making and breaking disulfide bonds. Annu Rev Microbiol 51, 179-202.
2. Grauschopf U, Fritz A, Glockshuber R (2003) Mechanism of the electron transfer catalyst DsbB from Escherichia coli. EMBO J 22, 3503-13.
3. Messens J, Collet JF (2006) Pathways of disulfide bond formation in Escherichia coli. Int J Biochem Cell Biol 38, 1050-62.
4. Missiakas D, Schwager F, Raina S (1995) Identification and characterization of a new disulfide isomeraselike protein (DsbD) in Escherichia coli. EMBO J 14, 3415-24.
5. Andersen CL, Matthey-Dupraz A, Missiakas D, Raina S (1997) A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins. Mol Microbiol 26, 121-32. (Pubitemid 27438243)
6. Bessette PH, Cotto JJ, Gilbert HF, Georgiou G (1999) In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG. J Biol Chem 274, 7784-92.
7. Hiniker A, Bardwell JC (2004) In vivo substrate specificity of periplasmic disulfide oxidoreductases. J Biol Chem 279, 12967-73. (Pubitemid 38445872)
8. Hillson DA, Lambert N, Freedman RB (1984) Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase. Meth Enzymol 107, 281-94.
9. Lyles MM, Gilbert HF (1991) Catalysis of me oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30, 613-9.
10. Ramírez P, Toledo H, Giliani N, Jerez CA (2002) An exported Rhodanese-like protein is induced during growth of Acidithiobacillus ferrooxidans in metal sulfides and different sulfur compounds. Appl Environ Microbiol 68, 1837-45.
11. Chi A, Valenzuela L, Beard S, Mackey AJ, Shabanowitz J, Hunt DF, Jerez CA (2007) Periplasmic proteins of the extremophile Acidithiobacillus ferrooxidans: a high throughput proteomic analysis. Mol Cell Proteomics 6, 2239-51.
12. Heras B, Edeling MA, Schirra HJ, Raina S, Martin JL (2004) Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. Proc Natl Acad Sci USA 101, 8876-81.
13. Rawlings D (2005) Characteristics and adaptability of iron- and sulfur-oxidizing microorganisms used for the recovery of metals from minerals and their concentrates. Microb Cell Factories 4, 13
14. Rohwerder T, Sand W (2003) The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp. Microbiology 149, 1699-710.