Thioredoxin affinity chromatography: A useful method for further understanding the thioredoxin network

Journal of Experimental Botany

Volumn 56, Issue 416, 2005, Pages 1463-1468

  Hisabori, Toru ^a,b   Hara, Satoshi ^a   Fujii, Tetsufumi ^a   Yamazaki, Daisuke ^a   Hosoya Matsuda, Naomi ^a   Motohashi, Ken ^a,b  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

Disulphide bond; Protein protein interaction; Redox regulation; Thioredoxin; Thioredoxin affinity chromatography

Indexed keywords

BIODIVERSITY; CELLS; CHROMATOGRAPHY; REDOX REACTIONS;

CELLULAR COMPARTMENTS; ORGANELLES; THIOREDOXIN AFFINITY CHROMATOGRAPHY;

PROTEINS;

THIOREDOXIN; VEGETABLE PROTEIN;

AFFINITY CHROMATOGRAPHY; CHLOROPLAST; CYTOSOL; METABOLISM; METHODOLOGY; PLANT; REVIEW;

CHLOROPLASTS; CHROMATOGRAPHY, AFFINITY; CYTOSOL; PLANT PROTEINS; PLANTS; THIOREDOXIN;

EID: 20044391221     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/eri170     Document Type: Review

References (46)

1. Baalmann E, Backhausen JE, Rak C, Vetter S, Scheibe R. 1995. Reductive modification and nonreductive activation of purified spinach chloroplast NADP-dependent glyceraldehyde-3-phosphate dehydrogenase. Archives of Biochemistry and Biophysics 324, 201-208.
2. Bald D, Noji H, Yoshida M, Hirono-Hara Y, Hisabori T. 2001. Redox regulation of the rotation of F(1)-ATP synthase. Journal of Biological Chemistry 276, 39505-39507.
3. Balmer Y, Koller A, del Val G, Manieri W, Schürmann P, Buchanan BB. 2003. Proteomics gives insight into the regulatory function of chloroplast thioredoxins. Proceedings of the National Academy of Sciences, USA 100, 370-375.
4. Balmer Y, Koller A, Val GD, Schürmann P, Buchanan BB. 2004a. Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynthesis Research 79, 275-280.
5. Balmer Y, Vensel WH, Tanaka CK, et al. 2004b. Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria. Proceedings of the National Academy of Sciences, USA 101, 2642-2647.
6. Brandes HK, Larimer FW, Geck MK, Stringer CD, Schürmann P, Hartman FC. 1993. Direct identification of the primary nucleophile of thioredoxin f. Journal of Biological Chemistry 268, 18411-18414.
7. Broin M, Cuine S, Eymery F, Rey P. 2002. The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin involved in the protection of the photosynthetic apparatus against oxidative damage. The Plant Cell 14, 1417-1432.
8. 2 assimilation in oxygenic photosynthesis: the ferredoxin/thioredoxin system. Perspective on its discovery, present status, and future development. Archives of Biochemistry and Biophysics 288, 1-9.
9. Capitani G, Markovic-Housley Z, DelVal G, Morris M, Jansonius JN, Schürmann P. 2000. Crystal structures of two functionally different thioredoxins in spinach chloroplasts. Journal of Molecular Biology 302, 135-154.
10. Chinnawirotpisan P, Matsushita K, Toyama H, Adachi O, Limtong S, Theeragool G. 2003. Purification and characterization of two NAD-dependent alcohol dehydrogenases (ADHs) induced in the quinoprotein ADH-deficient mutant of Acetobacter pasteurianus SKU1108. Bioscience, Biotechnology and Biochemistry 67, 958-965.
11. Eklund H, Cambillau C, Sjoberg BM, Holmgren A, Jornvall H, Hoog JO, Branden CI. 1984. Conformational and functional similarities between glutaredoxin and thioredoxins. EMBO Journal 3, 1443-1449.
12. Goyer A, Haslekas C, Miginiac-Maslow M, Klein U, Le Marechal P, Jacquot JP, Decottignies P. 2002. Isolation and characterization of a thioredoxin-dependent peroxidase from Chlamydomonas reinhardtii. European Journal of Biochemistry 269, 272-282.
13. Hosoya-Matsuda N, Motohashi K, Yoshimura H, Nozaki A, Inoue K, Ohmori M, Hisabori T. 2005. Anti-oxidative stress system in cyanobacteria: significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803. Journal of Biological Chemistry 280, 840-846.
14. Jacquot JP, Lancelin JM, Meyer Y. 1997. Thioredoxins: structure and function in plant cells. New Phytologist 136, 543-570.
15. Johansson K, Ramaswamy S, Saarinen M, Lemaire-Chamley M, Issakidis-Bourguet E, Miginiac-Maslow M, Eklund H. 1999. Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form. Biochemistry 38, 4319-4326.
16. Kadokura H, Tian H, Zander T, Bardwell JC, Beckwith J. 2004. Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. Science 303, 534-537.
17. Katti SK, Robbins AH, Yang Y, Wells WW. 1995. Crystal structure of thioltransferase at 2.2 Å resolution. Protein Science 4, 1998-2005.
18. Koumoto Y, Shimada T, Kondo M, Takao T, Shimonishi Y, Hara-Nishimura I, Nishimura M. 1999. Chloroplast Cpn20 forms a tetrameric structure in Arabidopsis thaliana. The Plant Journal 17, 467-477.
19. Kozaki A, Kamada K, Nagano Y, Iguchi H, Sasaki Y. 2000. Recombinant carboxyltransferase responsive to redox of pea plastidic acetyl-CoA carboxylase. Journal of Biological Chemistry 275, 10702-10708.
20. Kozaki A, Mayumi K, Sasaki Y. 2001. Thiol-disulfide exchange between nuclear-encoded and chloroplast-encoded subunits of pea acetyl-CoA carboxylase. Journal of Biological Chemistry 276, 39919-39925.
21. Kumar JK, Tabor S, Richardson CC. 2004. Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli. Proceedings of the National Academy of Sciences, USA 101, 3759-3764.
22. Lee K, Lee J, Kim Y, Bae D, Kang KY, Yoon SC, Lim D. 2004. Defining the plant disulfide proteome. Electrophoresis 25, 532-541.
23. Lemaire SD, Guillon B, Le Marechal P, Keryer E, Miginiac-Maslow M, Decottignies P. 2004. New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii. Proceedings of the National Academy of Sciences, USA 101, 7475-7480.
24. Lindahl M, Florencio FJ. 2003. Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different. Proceedings of the National Academy of Sciences, USA 100, 16107-16112.
25. Marchand C, Le Marechal P, Meyer Y, Miginiac-Maslow M, Issakidis-Bourguet E, Decottignies P. 2004. New targets of Arabidopsis thioredoxins revealed by proteomic analysis. Proteomics 4, 2696-2706.
26. Martel R, Cloney LP, Pelcher LE, Hemmingsen SM. 1990. Unique composition of plastid chaperonin-60: alpha and beta polypeptide-encoding genes are highly divergent. Gene 94, 181-187.
27. Miginiac-Maslow M, Issakidis E, Lemaire M, Ruelland E, Jacquot JP, Decottignies P. 1997. Light-dependent activation of NADP-malate dehydrogenase: a complex process. Australian Journal of Plant Physiology 24, 529-542.
28. Mills JD, Mitchell P, Schürmann P. 1980. Modulation of coupling factor ATPase activity in intact chloroplasts, the role of the thioredoxin system. FEBS Letters 112, 173-177.
29. Motohashi K, Kondoh A, Stumpp MT, Hisabori T. 2001. Comprehensive survey of proteins targeted by chloroplast thioredoxin. Proceedings of the National Academy of Sciences, USA 98, 11224-11229.
30. Motohashi K, Koyama F, Nakanishi Y, Ueoka-Nakanishi H, Hisabori T. 2003. Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modulation of the peptidyl-prolyl cistrans isomerase activity. Journal of Biological Chemistry 278, 31848-31852.
31. Nalin CM, McCarty RE. 1984. Role of a disulfide bond in the gamma subunit in activation of the ATPase of chloroplast coupling factor 1. Journal of Biological Chemistry 259, 7275-7280.
32. Pastore D, Di Pede S, Passarella S. 2003. Isolated durum wheat and potato cell mitochondria oxidize externally added NADH mostly via the malate/oxaloacetate shuttle with a rate that depends on the carrier-mediated transport. Plant Physiology 133, 2029-2039.
33. Qin J, Clore GM, Gronenborn AM. 1994. The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure 2, 503-522.
34. Rey P, Cuine S, Eymery F, Garin J, Court M, Jacquot JP, Rouhier N, Broin M. 2005. Analysis of the proteins targeted by CDSP32, a plastidic thioredoxin participating in oxidative stress responses. The Plant Journal 41, 31-42.
35. Sasaki Y, Kozaki A, Hatano M. 1997. Link between light and fatty acid synthesis: thioredoxin-linked reductive activation of plastidic acetyl-CoA carboxylase. Proceedings of the National Academy of Sciences, USA 94, 11096-11101.
36. Scheibe R, Anderson LE. 1981. Dark modulation of NADP-dependent malate dehydrogenase and glucose-6-phosphate dehydrogenase in the chloroplast. Biochimica et Biophysica Acta 636, 58-64.
37. Schürmann P. 1995. Ferredoxin: thioredoxin system. Methods in Enzymology 252, 274-283.
38. Stumpp MT, Motohashi K, Hisabori T. 1999. Chloroplast thioredoxin mutants without active-site cysteines facilitate the reduction of the regulatory disulphide bridge on the gamma-subunit of chloroplast ATP synthase. Biochemistry Journal 341, 157-163.
39. 1-ATPase by the mutation at the regulatory region on the gamma subunit of chloroplast ATP synthase. Journal of Biological Chemistry 279, 16272-16277.
40. Verdoucq L, Vignols F, Jacquot JP, Chartier Y, Meyer Y. 1999. In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. Journal of Biological Chemistry 274, 19714-19722.
41. Wong JH, Balmer Y, Cai N, Tanaka CK, Vensel WH, Hurkman WJ, Buchanan BB. 2003. Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics. FEBS Letters 547, 151-156.
42. Wong JH, Cai N, Balmer Y, Tanaka CK, Vensel WH, Hurkman WJ, Buchanan BB. 2004. Thioredoxin targets of developing wheat seeds identified by complementary proteomic approaches. Phytochemistry 65, 1629-1640.
43. Yamazaki D, Motohashi K, Kasama T, Hara Y, Hisabori T. 2004. Target proteins of the cytosolic thioredoxins in Arabidopsis thaliana. Plant and Cell Physiology 45, 18-27.
44. Yano H, Wong JH, Lee YM, Cho MJ, Buchanan BB. 2001. A strategy for the identification of proteins targeted by thioredoxin. Proceedings of the National Academy of Sciences, USA 98, 4794-4799.
45. Zhang N, Kallis RP, Ewy RG, Portis Jr AR. 2002. Light modulation of Rubisco in Arabidopsis requires a capacity for redox regulation of the larger Rubisco activase isoform. Proceedings of the National Academy of Sciences, USA 99, 3330-3334.
46. Zhang N, Portis Jr AR. 1999. Mechanism of light regulation of Rubisco: a specific role for the larger Rubisco activase isoform involving reductive activation by thioredoxin-f. Proceedings of the National Academy of Sciences, USA 96, 9438-9443.