Mouse glutaredoxin - cDNA cloning, high level expression in E. coli and its possible implication in redox regulation of the DNA binding activity in transcription factor PEBP2

Free Radical Research

Volumn 31, Issue 4, 1999, Pages 357-365

  Nakamura, Takayuki ^a   Ohno, Tetsuya ^a   Hirota, Kiichi ^a   Nishiyama, Akira ^a   Nakamura, Hajime ^a   Wada, Hiromi ^a   Yodoi, Junji ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

DNA binding activity; Glutaredoxin; PEBP2; Redox regulation; Transcription factor

Indexed keywords

GLUTAREDOXIN; GLUTATHIONE DISULFIDE; MUTANT PROTEIN; OXIDOREDUCTASE; THIOREDOXIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR PEBP2; TRANSFERASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; CONFERENCE PAPER; CONTROLLED STUDY; DNA BINDING; DNA LIBRARY; DNA TRANSFECTION; ELECTROPHORETIC MOBILITY; ESCHERICHIA COLI; MOLECULAR CLONING; MOLECULAR WEIGHT; MOUSE; NONHUMAN; OXIDATION REDUCTION REACTION;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; DNA; DNA, COMPLEMENTARY; DNA-BINDING PROTEINS; ESCHERICHIA COLI; MICE; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; OXIDATIVE STRESS; OXIDOREDUCTASES; PROTEINS; TRANSCRIPTION FACTOR AP-2; TRANSCRIPTION FACTORS;

ANIMALIA; ESCHERICHIA COLI; MAMMALIA; RODENTIA;

EID: 0032827583     PISSN: 10715762     EISSN: None     Source Type: Journal    
DOI: 10.1080/10715769900300931     Document Type: Conference Paper

References (43)

1. J. Yodoi and T. Uchiyama (1992) Diseases associated with HTLV-I:virus, IL-2 receptor dysregulation and redox regulation. Immunology Today 13, 405-411.
2. H. Nakamura, K. Nakamura and J. Yodoi (1997) Redox regulation of cellular activation. Annual Reviews of Immunology 15, 351-369.
3. W.W. Wells, Y. Yang, T.L. Deits and Z.R. Gan (1993) Thioltransferases. Advances in Enzymology 66, 149-201.
4. J.V. Höög, H. Jörnvall, A. Holmgren, M. Carlquist and M. Persson (1983) The primary structure of Escherichia coli glutaredoxin. European Journal of Biochemistry 136, 223-232.
5. Y.F. Yang and W.W. Wells (1990) High-level expression of pig liver thioltransferase (glutaredoxin) in Escherichia coli. Journal of Biological chemistry 265, 589-593.
6. C.A. Padilla, E. Martinez Galisteo, J.A. Barcena, G. Spyrou and A. Holmgren (1995) Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin. European Journal of Biochemistry 227, 27-34.
7. V.V. Papov, S.A. Gravina, J.J. Mieyal and K. Biemann (1994) The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells. Protein Science 3, 428-434.
8. J.B. Park and M. Levine (1996) Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin. Biochemical Journal 315, 931-938.
9. Z.R. Gan and W.W. Wells (1987) The primary structure of pig liver thioltransferase. Journal of Biological Chemistry 262, 6699-6703.
10. I.A. Papayannopoulos, Z.R. Gan, W.W. Wells and K. Biemann (1989) A revised sequence of calf thymus glutaredoxin. Biochemical and Biophysical Research Communications 159, 1448-1454.
11. S. Hopper, R.S. Johnson, J.E. Vath and K. Biemann (1989) Glutaredoxin from rabbit bone marrow. Purification, characterization, and amino acid sequence determined by tandem mass spectrometry. Journal of Biological Chemistry 264, 20438-20447.
12. M. Luthman and A. Holmgren (1982) Glutaredoxin from calf thymus. Purification to homogeneity. Journal of Biological Chemistry 257, 6686-6690.
13. A. Holmgren (1989) Thioredoxin and glutaredoxin systems. Journal of Biological Chemistry 264, 13963-13966.
14. A. Holmgren (1978) A thiol-dependent transhydrogenase from yeast. Journal of Biological Chemistry 253, 7424-7430.
15. A. Holmgren (1976) Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proceedings of the National Academy of Sciences of the USA 73, 2275-2279.
16. J.J. Mieyal, D.W. Starke, S.A. Gravina, C. Dothey and J.S. Chung (1991) Thioltransferase in human red blood cells: purification and properties. Biochemistry 30, 6088-6097.
17. T. Terada, T. Oshida, M. Nishimura, H. Maeda, T. Hara, S. Hosomi, T. Mizoguchi and T. Nishihara (1992) Study on human erythrocyte thioltransferase: comparative characterization with bovine enzyme and its physiological role under oxidative stress. Journal of Biochemistry (Tokyo) 111, 688-692.
18. S. Yoshitake, H. Nanri, M.R. Fernando and S. Minakami (1994) Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins. Journal of Biochemistry (Tokyo) 116, 42-46.
19. H.F. Gilbert (1990) Molecular and cellular aspects of thiol-disulfide exchange. Advances in Enzymology 63, 69-172.
20. Y. Tagaya, Y. Maeda, A. Mitsui, N. Kondo, H. Matsui, J. Hamuro, N. Brown, K. Arai, T. Yokota, H. Wakasugi and J. Yodoi (1989) ATL-deived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; Possible involvement of dithiol-reduction in the IL-2 receptor induction. EMBO Journal 8, 757-764.
21. C.A. Chrestensen, C.B. Eckman, D.W. Starke and J.J. Mieyal (1995) Cloning, expression and characterization of human thioltransferase (glutaredoxin) in E. coli. FEBS Letters 374, 25-28.
22. M.R. Fernando, H. Sumimoto, H. Nanri, S. Kawabata, S. Iwanaga, S. Minakami, Y. Fukumaki and K. Takeshige (1994) Cloning and sequencing of the cDNA encoding human glutaredoxin. Biochimica et Biophysica Acta 1218, 229-231.
23. Y.F. Yang, Z.R. Gan and W.W. Wells (1989) Cloning and sequencing the cDNA encoding pig liver thioltransferase. Gene 83, 339-346, issn: 0378-1119.
24. K. Sorachi, K. Sugie, N. Maekawa, M. Takami, T. Kawabe, S. Kumagai, H. Imura and J. Yodoi (1992) Induction and function of Fc epsilon RII on YT cells; possible role of ADF/thioredoxin in Fc epsilon RII expression. Immunobiology 185, 193-206.
25. T. Okamoto, H. Ogiwara, T. Hayashi, A. Mitsui, T. Kawabe and J. Yodoi (1992) Human thioredoxin/adult T cell leukemia-derived factor activates the enhancer binding protein of human immunodeficiency virus type 1 by thiol redox control mechanism. Internatioanl Immunology 4, 811-819.
26. T. Hayashi, Y. Ueno and T. Okamoto (1993) Oxidoreductive regulation of nuclear factor kappa B. Involvement of a cellular reducing catalyst thioredoxin. Journal of Biological Chemistry 268, 11380-11388.
27. C. Abate, L. Patel, F.J.d. Rauscher and T. Curran (1990) Redox regulation of fos and jun DNA-binding activity in vitro. Science 249, 1157-1161.
28. S. Xanthoudakis, G. Miao, F. Wang, Y.C. Pan and T. Curran (1992) Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO Journal 11, 3323-3335.
29. Y. Makino, K. Okamoto, N. Yoshikawa, M. Aoshima, K. Hirota, J. Yodoi, K. Umesono, I. Makino and H. Tanaka (1996) Thioredoxin: a redox-regulating cellular cofactor for glucocorticoid hormone action, Crosstalk between endocrine control of strees response and cellular antioxidant defense system. Journal of Clinical Investigation 98, 2469-2477.
30. H. Kagoshima, Y. Akamatsu, Y. Ito and K. Shigesada (1996) Functional dissection of the alpha and beta subunits of transcription factor PEBP2 and the redox susceptibility of its DNA binding activity. Journal of Biological Chemistry 271, 33074-33082.
31. S. Xanthoudakis and T. Curran (1992) Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO Journal 11, 653-665.
32. Y. Akamatsu, T. Ohno, K. Hirota, H. Kagoshima, J. Yodoi and K. Shigesada (1997) Redox regulation of DNA binding activity in transcription factor PEBP2. Journal of Biological Chemistry 272, 14497-14500.
33. I.M. Klintrot, J.O. Höög, H. Jörnvall, A. Holmgren and M. Luthman (1984) The primary structure of calf thymus glutaredoxin. Homology with the corresponding Escherichia coli protein but elongation at both ends and with an additional half-cystine/cysteine pair structure of calf thymus glutaredoxin European Journal of Biochemistry 144, 417-423.
34. Y.F. Yang and W.W. Wells (1991) Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis. Journal of Biological Chemistry 266, 12759-12765.
35. E. Ogawa, M. Maruyama, H. Kagoshima, M. Inuzuka, J. Lu, M. Satake, K. Shigesada and Y. Ito (1983) PEBP2/PEA2 represents a family of transcription factors homologous to the products of the Drosophila runt gene and the human AML1 gene. Proceedings of the National Academy of Sciences of the USA 90, 6859-6863.
36. N.A. Speck and S. Terryl (1995) A new transcription factor family associated with human leukemias. Critical Reviews in Eukaryotic Gene Expression 5, 337-364.
37. S. Wang, Q. Wang, B.F. Crute, I.N. Melnikova, S.R. Keller and N.A. Speck (1993) Cloning and characterization of subunits of the T-cell receptor and murine leukemia virus enhancer core-binding factor. Molecular Cell Biology 13, 3324-3339.
38. M.A. Kania, A.S. Bonner, J.B. Duffy and J.P. Gergen (1990) The drosophila segmentation gene runt encodes a novel nuclear regulatory protein that is also expressed in the developing nervous system. Genes and Development 4, 1701-1713.
39. H. Miyoshi, K. Shimizu, T. Kozu, N. Maseki, Y. Kaneko and M. Ohki (1991) t(8;21) breakpoints on chromosome 21 in acute myeloid leukemia are clustered within a limited region of a single gene, AML1. Proceedings of National Academy of Sciences of the USA 88, 10431-10434.
40. H. Kagoshima, K. Shigesada, M. Satake, Y. Ito, H. Miyoshi, M. Ohki, M. Pepling and P. Gergen (1993). The Runt domain identifies a new family of heteromeric transcriptional regulators. Trends in Genetics 9, 338-341.
41. S.B. Bandyopadhyay, D.W. Starke, J.J. Mieyal and R.M. Gronostajski (1997) Thioltransferase (Glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated Nuclear Factor I. Journal of Biological Chemistry 273, 392-397.
42. M. Zheng, F. Asulund and G. Storz (1998) Activation of the OxyR transcription factor by reversible disulfidebond formation. Science 279, 1718-1721.
43. U. Srinivasan, P.A. Mieyal and J.J. Mieyal (1997) pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis. Biochemistry 36, 3199-3206.