The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux

König, Janine; Baier, Margarete; Horling, Frank; Kahmann, Uwe; Harris, Gary C.; Schürmann, Peter; Dietz, Karl‐Josef

doi:10.1073/pnas.072644999

Cited by 281 publications

(296 citation statements)

References 27 publications

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“…2-Cys PRXs, including PRX-I, is known to form obligate homodimers (Wood et al, 2003). The main band and the ladder bands should correspond to the dimer and oligomer forms of PRX-I, respectively, because a very similar pattern was reported previously in the case of plant 2-Cys PRX (Ko¨nig et al, 2002). By contrast, C173S PRX-I constitutively formed oligomers but C51S or C83S PRX-I did not form oligomers even in the presence of H 2 O 2 .…”

Section: Resultssupporting

confidence: 70%

Oligomeric peroxiredoxin-I is an essential intermediate for p53 to activate MST1 kinase and apoptosis

et al. 2011

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Mammalian Ste20-like kinase-1 (MST1) kinase mediates H 2 O 2 -induced cell death by anticancer drugs such as cisplatin in a p53-dependent manner. However, the mechanism underlying MST1 activation by H 2 O 2 remains unknown. Here we show that peroxiredoxin-I (PRX-I) is an essential intermediate in H 2 O 2 -induced MST1 activation and cisplatin-induced cell death through p53. Cell stimulation with H 2 O 2 resulted in PRX-I oxidation to form homo-oligomers and interaction with MST1, leading to MST1 autophosphorylation and augmentation of kinase activity. In addition, RNA interference knockdown experiments indicated that endogenous PRX-I is required for H 2 O 2 -induced MST1 activation. Live-cell imaging showed H 2 O 2 generation by cisplatin treatment, which likewise caused PRX-I oligomer formation, MST1 activation and cell death. Cisplatin-induced PRX-I oligomer formation was not observed in embryonic fibroblasts obtained from p53-knockout mice, confirming the importance of p53. Indeed, ectopic expression of p53 induced PRX-I oligomer formation and cell death, both of which were cancelled by the antioxidant NAC. Moreover, we succeeded in reconstituting H 2 O 2 -induced MST1 activation in vitro, using purified PRX-I and MST1 proteins. Collectively, our results show a novel PRX-I function to cause cell death in response to high levels of oxidative stress by activating MST1, which underlies the p53-dependent cytotoxicity caused by anticancer agents.

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Section: Resultssupporting

confidence: 70%

Oligomeric peroxiredoxin-I is an essential intermediate for p53 to activate MST1 kinase and apoptosis

et al. 2011

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“…2-Cys Prxs also detoxify peroxides within the chloroplast Konig et al, 2002). The chloroplast is the main source of ROS due to its role in photosynthesis and the synthesis of amino acids, fatty acids and nucleotides (Apel et al, 2004).…”

Section: Srx and Chlroplast Protectionmentioning

confidence: 99%

The Peroxiredoxin Repair Proteins

Jönsson

Lowther

2007

Subcellular Biochemistry

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Sulfiredoxin and sestrin are cysteine sulfinic acid reductases that selectively reduce or repair the hyperoxidized forms of typical 2-Cys peroxiredoxins within eukaryotes. As such these enzymes play key roles in the modulation of peroxide-mediated cell signaling and cellular defense mechanisms. The unique structure of sulfiredoxin facilitates access to the peroxiredoxin active site and novel sulfur chemistry.

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“…Therefore we assume that the protein is attached to the thylakoid membrane by the C terminus. Studies on a peroxiredoxin protein indicated that the decameric form was attached to the thylakoid membrane, and this depended on the physiological status of the cell (Konig et al, 2002). Future experiments need to be done to explain the function of the membrane-associated AtStr15 protein.…”

Section: Organellementioning

confidence: 99%

Intracellular Localization of Arabidopsis Sulfurtransferases

Bauer

Dietrich²,

Nowak³

et al. 2004

Plant Physiology

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Sulfurtransferases (Str) comprise a group of enzymes widely distributed in archaea, eubacteria, and eukaryota which catalyze the transfer of a sulfur atom from suitable sulfur donors to nucleophilic sulfur acceptors. In all organisms analyzed to date, small gene families encoding Str proteins have been identified. The gene products were localized to different compartments of the cells. Our interest concerns the localization of Str proteins encoded in the nuclear genome of Arabidopsis. Computer-based prediction methods revealed localization in different compartments of the cell for six putative AtStrs. Several methods were used to determine the localization of the AtStr proteins experimentally. For AtStr1, a mitochondrial localization was demonstrated by immunodetection in the proteome of isolated mitochondria resolved by one-and two-dimensional gel electrophoresis and subsequent blotting. The respective mature AtStr1 protein was identified by mass spectrometry sequencing. The same result was obtained by transient expression of fusion constructs with the green fluorescent protein in Arabidopsis protoplasts, whereas AtStr2 was exclusively localized to the cytoplasm by this method. Three members of the single-domain AtStr were localized in the chloroplasts as demonstrated by transient expression of green fluorescent protein fusions in protoplasts and stomata, whereas the single-domain AtStr18 was shown to be cytoplasmic. The remarkable subcellular distribution of AtStr15 was additionally analyzed by transmission electron immunomicroscopy using a monospecific antibody against green fluorescent protein, indicating an attachment to the thylakoid membrane. The knowledge of the intracellular localization of the members of this multiprotein family will help elucidate their specific functions in the organism.All members in the sulfurtransferase (Str)/rhodanese protein family in archaea, eubacteria, and eukaryota are unified by characteristic well-defined sequence domains (Bordo and Bork, 2002). These domains are found as tandem repeats, with the C-terminal domain containing the active site Cys residue, as singledomain proteins or as members of multidomain proteins (Bordo and Bork, 2002). The 18 proteins identified in Arabidopsis which contain at least one Str signature were classified into six groups on the basis of their sequence homology (Bauer and Papenbrock, 2002; http://arabidopsis.org/info/ genefamily/STR_genefamily.html). Group I consists of two Str proteins with two-domain; the five proteins in group VI contain only the C-terminal Str signature and thus possess similarity to the single-domain Str from bacteria.Strs catalyze the transfer of a sulfur atom from suitable sulfur donors to a nucleophilic acceptor. Specific biological roles for most members of this superfamily have not been established (Spallarossa et al., 2001). Proposed roles include cyanide detoxification (Vennesland et al., 1982), involvement in sulfate assimilation (Donadio et al., 1990), and mobilization of sulfur for iron-sulfur cluster biosynthes...

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The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux

Cited by 281 publications

References 27 publications

Oligomeric peroxiredoxin-I is an essential intermediate for p53 to activate MST1 kinase and apoptosis

Oligomeric peroxiredoxin-I is an essential intermediate for p53 to activate MST1 kinase and apoptosis

The Peroxiredoxin Repair Proteins

Intracellular Localization of Arabidopsis Sulfurtransferases

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