Thioredoxin peroxidase in the Cyanobacterium Synechocystis sp. PCC 6803

FEBS Letters

Volumn 447, Issue 2-3, 1999, Pages 269-273

  Yamamoto, Hiroshi ^a,b,c   Miyake, Chikahiro ^d   Dietz, Karl Josef ^e   Tomizawa, Ken Ichi ^a   Murata, Norio ^b,c   Yokota, Akiho ^a,d  

^a RESEARCH INSTITUTE OF INNOVATIVE TECHNOLOGY FOR THE EARTH   (Japan)

^b GRADUATE UNIVERSITY FOR ADVANCED STUDIES   (Japan)

^c NATIONAL INSTITUTE FOR BASIC BIOLOGY   (Japan)

^d NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^e BIELEFELD UNIVERSITY   (Germany)

Author keywords

Chlorophyll fluorescence; Cyanobacterium; Hydrogen peroxide; Synechocystis sp. PCC 6803; Thioredoxin peroxidase

Indexed keywords

HYDROGEN PEROXIDE; PEROXIDASE; THIOREDOXIN; THIOREDOXIN PEROXIDASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CYANOBACTERIUM; ELECTRON TRANSPORT; FLUORESCENCE; NONHUMAN; OPEN READING FRAME; PHOTOSYSTEM II; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; BASE SEQUENCE; CYANOBACTERIA; DNA PRIMERS; ELECTRON TRANSPORT; ESCHERICHIA COLI; GENE EXPRESSION; GENES, BACTERIAL; HYDROGEN PEROXIDE; MOLECULAR SEQUENCE DATA; NEOPLASM PROTEINS; OPEN READING FRAMES; PEROXIDASES; PHOTOSYNTHESIS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TERT-BUTYLHYDROPEROXIDE;

ESCHERICHIA COLI; SYNECHOCYSTIS SP.; SYNECHOCYSTIS SP. PCC 6803;

EID: 0032971732     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(99)00309-9     Document Type: Article

References (26)

1. Halliwell, B. and Gutteridge, J.M.C. (1989) Free Radicals in Biology and Medicine, Clarendon Press, Oxford.
2. Asada, K., Endo, T., Mano, J. and Miyake, C. (1998) in: Stress Responses of Photosynthetic Organisms - Molecular Mechanisms and Molecular Regulations (Satoh, K. and Murata, N., Eds.), pp. 37-52, Elsevier Science, Tokyo.
3. Miyake C., Michihata F., Asada K. Plant Cell Physiol. 32:1991;33-43.
4. Asada, K. (1994) in: Cause of Photooxidative Stress and Amelioration of Defense Systems in Plants (Foyer, C.H. and Mullineaux, P.M., Eds.), pp. 77-104, CRC Press, London.
5. Kim K., Kim I.H., Lee K.Y., Rhee S.G., Stadtman E.R. J. Biol. Chem. 263:1988;4704-4711.
6. Chae H.Z., Sang J.C., Rhee S.G. J. Biol. Chem. 269:1994;27670-27678.
7. Cha M.K., Kim H.K., Kim H.I. J. Biol. Chem. 270:1995;28635-28641.
8. Baier M., Dietz K.J. Plant Mol. Biol. 31:1996;553-564.
9. Baier M., Dietz K.J. Plant J. 12:1997;179-190.
10. Kaneko T., Tabata S. Plant Cell Physiol. 38:1997;1171-1176.
11. Bradford M.M. Anal. Biochem. 72:1976;248-254.
12. Laemmli U.K. Nature. 227:1970;680-685.
13. Elhai J., Wolk C.P. Gene. 68:1988;119-138.
14. Williams, J.G.K. (1988) in: Method in Enzymology (Packer, L. and Glazer, A.N., Eds.), Vol. 167, pp. 766-778, Academic Press, New York.
15. Miller A.G., Canvin D.T. Biochim. Biophys. Acta. 894:1987;407-413.
16. Badger M.R., Schreiber U. Photosynth. Res. 37:1993;177-191.
17. Chae H.Z., Uhm T.B., Rhee S.G. Proc. Natl. Acad. Sci. USA. 91:1994;7022-7026.
18. Kim I.H., Kim K., Rhee S.G. Proc. Natl. Acad. Sci. USA. 86:1989;6018-6022.
19. Lim Y.S., Cha M.K., Kim H.K., Kim I.H. Gene. 140:1994;279-284.
20. Choi H.J., Kang S.W., Yang C.H., Rhee S.G., Ryu S.E. Nat. Struct. Biol. 5:1998;400-406.
21. Mutsuda M., Ishikawa T., Takeda T., Shigeoka S. Biochem. J. 316:1996;251-257.
22. Holland D., Faltin Z., Perl A., Ben-Hayyim G., Eshdat Y. FEBS Lett. 337:1994;52-55.
23. Yokota A., Shigeoka S., Onishi T., Kitaoka S. Plant Physiol. 86:1988;649-651.
24. Chae H.Z., Kim H.I., Kanghwa K., Rhee S.G. J. Biol. Chem. 268:1993;16815-16821.
25. Cha M.K., Kim H.K., Kim I.H. J. Bacteriol. 178:1996;5610-5614.
26. Pearson W.R., Lipman D.J. Proc. Natl. Acad. Sci. USA. 85:1988;2444-2448.