Triple mutation of Cys26, Trp35, and Cys126 in stromal ascorbate peroxidase confers H2O2 tolerance comparable to that of the cytosolic isoform

Biochemical and Biophysical Research Communications

Volumn 372, Issue 4, 2008, Pages 918-923

  Kitajima, Sakihito ^a   Kitamura, Masahito ^a   Koja, Namiko ^a  

^a KYOTO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

Ascorbate peroxidase; Chloroplast; Cysteine; Hydrogen peroxide; Inactivation; Radical; Stroma; Tryptophan

Indexed keywords

ASCORBATE PEROXIDASE; CYSTEINE; HYDROGEN PEROXIDE; TRYPTOPHAN;

ARTICLE; CYTOSOL; ENZYME INACTIVATION; ENZYME LOCALIZATION; MUTANT; MUTATION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL;

APOPROTEINS; CRYSTALLOGRAPHY, X-RAY; CYCLIC N-OXIDES; CYSTEINE; CYTOSOL; HYDROGEN PEROXIDE; ISOENZYMES; MUTATION; PEROXIDASES; PLANT PROTEINS; PORPHYRINS; PROTEIN CONFORMATION; TOBACCO; TRYPTOPHAN;

EID: 45449085829     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.05.160     Document Type: Article

References (21)

1. Asada K. The water-water cycle in chloroplasts: scavenging of active oxygens and dissipation of excess photons. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50 (1999) 601-639
2. Asada K. Production and scavenging of reactive oxygen species in chloroplasts and their functions. Plant Physiol. 141 (2006) 391-396
3. Chew O., Whelan J., and Millar A.H. Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria dual targeting of antioxidant defenses in plants. J. Biol. Chem. 278 (2003) 46869-46877
4. 2. FEBS J. 274 (2007) 3013-3020
5. Kitajima S., Tomizawa K., Shigeoka S., and Yokota A. An inserted loop region of stromal ascorbate peroxidase is involved in its hydrogen peroxide-mediated inactivation. FEBS J. 273 (2006) 2704-2710
6. Hiner A.N., Rodriguez-Lopez J.N., Arnao M.B., Raven E.L., Garcia-Canovas F., and Acosta M. Kinetic study of the inactivation of ascorbate peroxidase by hydrogen peroxide. Biochem. J. 348 (2000) 321-328
7. Kitajima S., Kurioka M., Yoshimoto T., Shindo M., Kanaori K., Tajima K., and Oda K. A cysteine residue near the propionate side-chain of heme is the radical site in ascorbate peroxidase. FEBS J. 275 (2008) 470-480
8. Smulevich G., Mauro J.M., Fishel L.A., English A.M., Kraut J., and Spiro T.G. Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroscopy. Biochemistry 26 (1988) 5477-5485
9. Goodin D.B., Davidson M.G., Roe J.A., Mauk A.G., and Smith M. Amino acid substitutions at tryptophan-51 of cytochrome c peroxidase: effects on coordination, species preference for cytochrome c, and electron transfer. Biochemistry 30 (1991) 4953-4962
10. Borisenko G.G., Martin I., Zhao Q., Amoscato A.A., and Kagan V.E. Nitroxides scavenge myeloperoxidase-catalyzed thiyl radicals in model systems and in cells. J. Am. Chem. Soc. 126 (2004) 9221-9232
11. Kitajima S., Ueda M., Sano S., Miyake C., Kohchi T., Tomizawa K., Shigeoka S., and Yokota A. Stable form of ascorbate peroxidase from the red alga Galdieria partita similar to both chloroplastic and cytosolic isoforms of higher plants. Biosci. Biotechnol. Biochem. 66 (2002) 2367-2375
12. Allen R.D. Dissection of oxidative stress tolerance using transgenic plants. Plant Physiol. 107 (1995) 1049-1054
13. Allen R.D., Webb R.P., and Schake S.A. Use of transgenic plants to study antioxidant defenses. Free Radic. Biol. Med. 23 (1997) 473-479
14. Torsethaugen G., Pitcher L.H., Zilinskas B.A., and Pell F.J. Overproduction of ascorbate peroxidase in the tobacco chloroplast does not provide protection against ozone. Plant Physiol. 114 (1997) 529-537
15. Payton P., Webb R., Kornyeyev D., Allen R., and Holaday A.S. Protecting cotton photosynthesis during moderate chilling at high light intensity by increasing chloroplastic antioxidant enzyme activity. J. Exp. Bot. 52 (2001) 2345-2354
16. Kornyeyev D., Logan B.A., Payton P., Allen R.D., and Holaday A.S. Enhanced photochemical light utilization and decreased chilling-induced photoinhibition of photosystem II in cotton overexpressing genes encoding chloroplast-targeted antioxidant enzymes. Physiol. Plant. 113 (2001) 323-331
17. Kornyeyev D., Logan B.A., Payton P., Allen R.D., and Holaday A.S. Effect of chloroplastic overproduction of ascorbate peroxidase on photosynthesis and photoprotection in cotton leaves subjected to low temperature photoinhibition. Plant Sci. 165 (2003) 1033-1041
18. Yabuta Y., Motoki T., Yoshimura K., Takeda T., Ishikawa T., and Shigeoka S. Thylakoid membrane-bound ascorbate peroxidase is a limiting factor of antioxidative systems under photo-oxidative stress. Plant J. 32 (2002) 915-925
19. Murgia I., Tarantino D., Vannini C., Bracale M., Carravieri S., and Soave C. Arabidopsis thaliana plants overexpressing thylakoidal ascorbate peroxidase show increased resistance to Paraquat-induced photooxidative stress and to nitric oxide-induced cell death. Plant J. 38 (2004) 940-953
20. Shigeoka S., Ishikawa T., Tamoi M., Miyagawa Y., Takeda T., Yabuta Y., and Yoshimura K. Regulation and function of ascorbate peroxidase isoenzymes. J. Exp. Bot. 53 (2002) 1305-1319
21. Wada K., Tada T., Nakamura Y., Ishikawa T., Yabuta Y., Yoshimura K., Shigeoka S., and Nishimura K. Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights into its instability. J. Biochem. 134 (2003) 239-244