Differential Regulation of Plastidial and Cytosolic Isoforms of Peptide Methionine Sulfoxide Reductase in Arabidopsis

Sadanandom, Arivananthan; Poghosyan, Zaruhi; Fairbairn, David J.; Murphy, Denis J.

doi:10.1104/pp.123.1.255

Cited by 84 publications

(69 citation statements)

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“…(From Karpinski et al 1999. ) Although a cytosolic and a plastidic form of PMSR have been described in plants (Sadanandom et al 2000), little information concerning their respective roles in antioxidant defense is yet available. A search for the in vivo substrates of PMSR in the peroxisome and the cytosol could yield valuable information.…”

Section: Prospects For Improving Stress Resistancementioning

confidence: 99%

Oxidative Stress and Acclimation Mechanisms in Plants

Grene

2002

The Arabidopsis Book

116

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Section: Prospects For Improving Stress Resistancementioning

confidence: 99%

Oxidative Stress and Acclimation Mechanisms in Plants

Grene

2002

The Arabidopsis Book

116

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“…Five MsrA-like genes were identified in Arabidopsis thaliana; one encodes chloroplastic isoforms, and another one is predicted to be targeted to the secretory pathway, and three are cytosolic enzymes (21,22). The expression of the chloroplastic isoform, found mainly in photosynthetic tissues, is strongly induced by illumination of etiolated seedlings and is responsive to various oxidative stress conditions (21)(22)(23). Moreover, this plastidial MsrA was also shown to maintain chaperonin activity of a small heat-shock protein Hsp21 by preventing its denaturation and consequently inactivation after methionine oxidation (24).…”

mentioning

confidence: 99%

“…Moreover, this plastidial MsrA was also shown to maintain chaperonin activity of a small heat-shock protein Hsp21 by preventing its denaturation and consequently inactivation after methionine oxidation (24). Finally, the expression of cytosolic MsrAs was also shown to respond to various changing conditions as follows: (i) in the dark period of A. thaliana plants growing in short-day conditions (25), (ii) during a pathogen infection by the cauliflower mosaic virus (21), or (iii) during softening of cold-hardened leaves (26). The previous reports about the plant MsrAs have focused essentially on their expression patterns, but the catalytic mechanism, in particular that related to Trx-dependent recycling process, and the three-dimensional structure of a plant MsrA have not yet been addressed.…”

mentioning

confidence: 99%

Functional and Structural Aspects of Poplar Cytosolic and Plastidial Type A Methionine Sulfoxide Reductases

Rouhier

Kauffmann

Favier

et al. 2007

Journal of Biological Chemistry

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The genome of Populus trichocarpa contains five methionine sulfoxide reductase A genes. Here, both cytosolic (cMsrA) and plastidial (pMsrA) poplar MsrAs were analyzed. The two recombinant enzymes are active in the reduction of methionine sulfoxide with either dithiothreitol or poplar thioredoxin as a reductant. signature specific for most plant MsrAs. The tyrosine residue corresponds to the one described to be involved in substrate binding in bacterial and B. taurus MsrAs. In these MsrAs, the tyrosine residue belongs to a similar signature as found in plant MsrAs but with the first C-terminal cysteine instead of the last C-terminal cysteine.The production and accumulation of reactive oxygen and nitrogen intermediates, inherent to metabolic processes such as respiration or photosynthesis or to stress conditions, initiate oxidative reactions that affect the biochemical constituents of the cells (1, 2). Living organisms use different strategies to prevent oxidative damage and lethal effects that would result from these compounds. Reactive species are trapped and degraded, or modifications that occur anyway are reversed by repair systems, and finally nonrepaired macromolecules can be degraded and removed. Methionine residues of proteins were shown to be one of the preferred targets of oxidation with the formation of methionine sulfoxide (MetSO) 3 (3). Enzymes named methionine sulfoxide reductases were found to catalyze the reduction of MetSO back to methionine residues (4, 5). The consequences of this side-chain modification are variable and can be partial to protein unfolding (6, 7) and modification of biological functions (8 -10). Sometimes surface methionine residues can undergo oxidation without much impact on the protein properties, and this modification can be seen as a mechanism to scavenge oxidative species in a detoxification process based on methionine sulfoxide reductase activity (11). Because of its asymmetric sulfur atom, MetSO exists as two stereoisomeric forms, Met-(S)-SO and Met-(R)-SO. Their reduction back to methionine is catalyzed by two structurally unrelated classes of Msr, MsrAs are specific for Met-(S)-SO, whereas Met-(R)-SO is the substrate of MsrBs.MsrAs and MsrBs display no significant sequence identity and have different three-dimensional structures. Only three MsrA x-ray structures from Escherichia coli, Bos taurus, and Mycobacterium tuberculosis and two MsrB structures from Neisseria species have been described so far (12-16). Both classes of Msrs share, for most of them, a similar three-step chemical mechanism, including the following: 1) a nucleophilic attack of the catalytic CysA residue on the sulfur atom of the sulfoxide substrate leading to the formation of a sulfenic acid intermediate and to the release of 1 mol of Met per mol of enzyme; 2) a formation of an intramonomeric disulfide bond between the catalytic CysA and the recycling CysB with a concomitant release of 1 mol of water; and 3) a reduction of the CysA-CysB methionine sulfoxide reductase disulfide bond by thioredoxin (Tr...

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“…Oxygen can also be added onto the methionine residue to form a methionine sulphoxide. The best characterized response to the oxidation of peptide residues is the induction of proteases that break down the oxidized proteins [93]. DNA damage, triggered by ROS is particularly dangerous for the cell since it causes replication errors and genomic instability.…”

Section: Reactive Oxygen Species In Plantsmentioning

confidence: 99%