The plant 2‐Cys peroxiredoxin BAS1 is a nuclear‐encoded chloroplast protein: its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants

Baier, Margarete; Dietz, Karl‐Josef

doi:10.1046/j.1365-313x.1997.12010179.x

Cited by 216 publications

(151 citation statements)

References 25 publications

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“…1 and supplemental Table 1). Among the prokaryotes with putative sensitive-type 2-Cys Prx are the cyanobacteria, the enzymes of which are related to those of algae and plants, confirming previous phylogenetic analysis (32). The only exception is the 2-Cys Prx from the cyanobacterium Gloeobacter violaceus, which lacks both the GG(L/V/I)G and the YF motifs (supplemental Table 1) and appears phylogenetically distant to 2-Cys Prxs from algae, plants, and other cyanobacteria (Fig.…”

Section: Discussionsupporting

confidence: 83%

Overoxidation of 2-Cys Peroxiredoxin in Prokaryotes

Pascual

Mata‐Cabana

Florencio

et al. 2010

Journal of Biological Chemistry

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In eukaryotic organisms, hydrogen peroxide has a dual effect; it is potentially toxic for the cell but also has an important signaling activity. According to the previously proposed floodgate hypothesis, the signaling activity of hydrogen peroxide in eukaryotes requires a transient increase in its concentration, which is due to the inactivation by overoxidation of 2-Cys peroxiredoxin (2-Cys Prx). Sensitivity to overoxidation depends on the structural GGLG and YF motifs present in eukaryotic 2-Cys Prxs and is believed to be absent from prokaryotic enzymes, thus representing a paradoxical gain of function exclusive to eukaryotic organisms. Here we show that 2-Cys Prxs from several prokaryotic organisms, including cyanobacteria, contain the GG(L/ V/I)G and YF motifs characteristic of sensitive enzymes. In search of the existence of overoxidation-sensitive 2-Cys Prxs in prokaryotes, we have analyzed the sensitivity to overoxidation of 2-Cys Prxs from two cyanobacterial strains, Anabaena sp. PCC7120 and Synechocystis sp. PCC6803. In vitro analysis of wild type and mutant variants of the Anabaena 2-Cys Prx showed that this enzyme is overoxidized at the peroxidatic cysteine residue, thus constituting an exception among prokaryotes. Moreover, the 2-Cys Prx from Anabaena is readily and reversibly overoxidized in vivo in response to high light and hydrogen peroxide, showing higher sensitivity to overoxidation than the Synechocystis enzyme. These cyanobacterial strains have different strategies to cope with hydrogen peroxide. While Synechocystis has low content of less sensitive 2-Cys Prx and high catalase activity, Anabaena contains abundant and sensitive 2-Cys Prx, but low catalase activity, which is remarkably similar to the chloroplast system.

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Section: Discussionsupporting

confidence: 83%

Overoxidation of 2-Cys Peroxiredoxin in Prokaryotes

Pascual

Mata‐Cabana

Florencio

et al. 2010

Journal of Biological Chemistry

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“…Peroxiredoxins are a family of enzymes that catalyze the transfer of electrons from sulfhydryl residues to peroxides and are ubiquitously distributed among all organisms [24]. Peroxiredoxins have diverse functions in cellular defense-signaling pathways [25], and 2-Cys peroxiredoxin plays direct roles in cellular-signaling events [25-27].…”

Section: Discussionmentioning

confidence: 99%

Phosphoproteins regulated by heat stress in rice leaves

Chen

Zhang

et al. 2011

Proteome Sci

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BackgroundHigh temperature is a critical abiotic stress that reduces crop yield and quality. Rice (Oryza sativa L.) plants remodel their proteomes in response to high temperature stress. Moreover, phosphorylation is the most common form of protein post-translational modification (PTM). However, the differential expression of phosphoproteins induced by heat in rice remains unexplored.MethodsPhosphoprotein in the leaves of rice under heat stress were displayed using two-dimensional electrophoresis (2-DE) and Pro-Q Diamond dye. Differentially expressed phosphoproteins were identified by MALDI-TOF-TOF-MS/MS and confirmed by Western blotting.ResultsTen heat-phosphoproteins were identified from twelve protein spots, including ribulose bisphos-phate carboxylase large chain, 2-Cys peroxiredoxin BAS1, putative mRNA binding protein, Os01g0791600 protein, OSJNBa0076N16.12 protein, putative H(+)-transporting ATP synthase, ATP synthase subunit beta and three putative uncharacterized proteins. The identification of ATP synthase subunit beta was further validated by Western-blotting. Four phosphorylation site predictors were also used to predict the phosphorylation sites and the specific kinases for these 10 phosphoproteins.ConclusionHeat stress induced the dephosphorylation of RuBisCo and the phosphorylation of ATP-β, which decreased the activities of RuBisCo and ATP synthase. The observed dephosphorylation of the mRNA binding protein and 2-Cys peroxiredoxin may be involved in the transduction of heat-stress signaling, but the functional importance of other phosphoproteins, such as H+-ATPase, remains unknown.

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“…1 h after the addition of 0.1-10 mM H 2 O 2 , the chloroplasts were sedimented at 3000 ϫ g. After removal of the supernatant, they were resuspended, lysed by the addition of 5 mM K-P i buffer (pH 7.5), and spun at 14,000 ϫ g. The supernatant was taken as stroma fraction, and the sedimented thylakoids were washed twice with K-P i buffer (pH 7.5) prior to resuspension in the same buffer. Volumes equivalent to 10 g of stroma and thylakoid proteins were analyzed by SDS-PAGE followed by Western blot using the Lumilight detection system (Roche Applied Science) and the BAS1 antibody specific to barley 2-Cys Prx (22). Detection of Inactivated 2-Cys Prx in Vivo-Leaf tissue was ground with sand in a buffer containing 125 mM Tris-HCl, pH 7.5, and 50 mM NaCl.…”

Section: Methodsmentioning

confidence: 99%

“…Membrane-Tissue fractionation demonstrated that 2-Cys Prx is post-translationally targeted to chloroplasts, where it was initially reported to reside in the stroma (22). Later, immunogold labeling indicated 72% thylakoid attachment at standard growth conditions (16).…”

Section: Reduction and Inactivation Mediates Attachment To The Thylakoidmentioning

confidence: 98%

Reaction Mechanism of Plant 2-Cys Peroxiredoxin

König¹,

Lotte

Plessow

et al. 2003

Journal of Biological Chemistry

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170

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Barley 2-cysteine peroxiredoxin (2-Cys Prx) was analyzed for peroxide reduction, quaternary structure, thylakoid attachment, and function as well as in vivo occurrence of the inactivated form, with emphasis on the role of specific amino acid residues. Data presented show the following. 1) 2-Cys Prx has a broad substrate specificity and reduces even complex lipid peroxides such as phosphatidylcholine dilineoyl hydroperoxide, although at low rates. 2) 2-Cys Prx partly becomes irreversibly oxidized by peroxide substrates during the catalytic cycle in a concentration-dependent manner, particularly by bulky hydroperoxides.

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The plant 2‐Cys peroxiredoxin BAS1 is a nuclear‐encoded chloroplast protein: its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants

Cited by 216 publications

References 25 publications

Overoxidation of 2-Cys Peroxiredoxin in Prokaryotes

Overoxidation of 2-Cys Peroxiredoxin in Prokaryotes

Phosphoproteins regulated by heat stress in rice leaves

Reaction Mechanism of Plant 2-Cys Peroxiredoxin

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