A peptide methionine sulfoxide reductase highly expressed in photosynthetic tissue in Arabidopsis thaliana can protect the chaperone-like activity of a chloroplast-localized small heat shock protein

Plant Journal

Volumn 29, Issue 5, 2002, Pages 545-553

  Gustavsson, Niklas ^a   Kokke, Bas P A ^b   Härndahl, Ulrika ^a   Silow, Maria ^a   Bechtold, Ulrike ^c   Poghosyan, Zaruhi ^d   Murphy, Denis ^c,e   Boelens, Wilbert C ^b   Sundby, Cecilia ^a  

^a LUND UNIVERSITY   (Sweden)

^b RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

^c UNIVERSITY OF GLAMORGAN   (United Kingdom)

^d UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^e Lipoprotein Research Centre   (United Kingdom)

Author keywords

Chaperone like activity; Methionine sulfoxidation; Oxidative stress; Peptide methionine sulfoxide reductase; Redox regulation; Small heat shock protein

Indexed keywords

CELLS; ENZYME KINETICS; GENES; PHOTOSYNTHESIS; TISSUE;

CELLULAR RESISTANCE;

PLANTS (BOTANY);

ARABIDOPSIS; ARABIDOPSIS THALIANA; EMBRYOPHYTA; EUKARYOTA;

ARABIDOPSIS PROTEIN; CHAPERONE; CITRATE SYNTHASE; DITHIOTHREITOL; DRUG DERIVATIVE; HEAT SHOCK PROTEIN; HSP21 PROTEIN, ARABIDOPSIS; ISOENZYME; METHIONINE; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE; OXIDOREDUCTASE; RECOMBINANT PROTEIN;

ARABIDOPSIS; ARTICLE; CHLOROPLAST; DRUG EFFECT; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; MASS SPECTROMETRY; METABOLISM; MUTATION; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PLANT LEAF; PLASTID; SITE DIRECTED MUTAGENESIS;

ARABIDOPSIS; ARABIDOPSIS PROTEINS; CHLOROPLASTS; CITRATE (SI)-SYNTHASE; DITHIOTHREITOL; ESCHERICHIA COLI; GENE EXPRESSION; HEAT-SHOCK PROTEINS; ISOENZYMES; METHIONINE; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; MUTATION; OXIDATION-REDUCTION; OXIDATIVE STRESS; OXIDOREDUCTASES; PLANT LEAVES; PLASTIDS; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 0036006188     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.2002.029005545.x     Document Type: Article

References (35)

1. Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity
2. Small stress proteins: Chaperones that act as regulators of intracellular redox state and programmed cell death
3. Gene expression and the thiol redox state
4. Enzymatic reduction of protein-bound methionine sulfoxide
5. The expanding small heat-shock protein family, and structure predictions of the conserved 'alpha-crystallin domain'
6. Analysis of conserved domains identifies a unique structural feature of a chloroplast heat shock protein
7. HIV 2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase
8. Degradation of active-oxygen-modified ribulose-1,5-bisphosphate carboxylase/oxygenase by chloroplastic proteases requires ATP-hydrolysis
9. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
10. Progressive decline in the ability of calmodulin isolated from aged brain to activate the plasma membrane Ca-ATPase
11. On the role of methionine residues in the sequence-independent recognition of non-polar protein surfaces
12. Repair of oxidized proteins: Identification of a new methionine sulfoxide reductase
13. Methionine sulfoxidation of the chloroplast small heat shock protein and conformational changes in the oligomer
14. Substitution of conserved methionines by leucines in chloroplast small heat shock protein results in loss of redox-response but retained chaperone-like activity
15. Alpha crystallin can function as a molecular chaperone
16. The chaperone-like activity of a small heat shock protein is lost after sulfoxidation of conserved methionines in a surface-exposed amphipathic alpha-helix
17. The chloroplast small heat shock protein-purification and characterization of pea recombinant protein
18. Small heat shock proteins are molecular chaperones
19. Systemic signaling and acclimation in response to excess excitation energy in Arabidopsis
20. Characterization of the methionine S-oxidase activity of rat liver and kidney microsomes: Immunochemical and kinetic evidence for FMO3 being the major catalyst
21. A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein
22. Methionine residues as endogenous antioxidants in proteins
23. One-electron photooxidation of N-methionyl peptides, mechanism of sulfoxide and azasulfonium diastereomer formation through reaction of sulfide radical cation complexes with oxygen or superoxide
24. Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
25. Escherichia coli peptide methionine sulfoxide reductase gene: Regulation of expression and role in protecting against oxidative damage
26. Cloning and expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins
27. A minimal gene set for cellular life derived by comparison of complete bacterial genomes
28. Identification of a peptide methionine sulphoxide reductase gene in a oleosin promoter from Brassica napus
29. Differential regulation of plastidial and cytosolic isoforms of peptide methionine sulfoxide reductase in Arabidopsis
30. Reduction of N-acetyl methionine sulfoxide in plants
31. Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase
32. Repair of oxidized calmodulin by methionine sulfoxide reductase restores the ability to activate the plasma membrane Ca-ATPase
33. Chloroplast small heat shock proteins: Evidence for atypical evolution of an organelle-localized protein
34. Oxidation of methionyl residues in proteins: Tools, targets, and reversal
35. Bridge over troubled waters: Sensing stress by disulfide formation