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Genome-wide analysis of thioredoxin fold superfamily peroxiredoxins in Arabidopsis and rice
Authors:Pavan Umate
Affiliation:Department of Botany, Kakatiya University; Warangal, India
Abstract:A broad range of peroxides generated in subcellular compartments, including chloroplasts, are detoxified with peroxidases called peroxiredoxins (Prx). The Prx are ubiquitously distributed in all organisms including bacteria, fungi, animals and also in cyanobacteria and plants. Recently, the Prx have emerged as new molecules in antioxidant defense in plants. Here, the members which belong to Prx gene family in Arabidopsis and rice are been identified. Overall, the Prx members constitute a small family with 10 and 11 genes in Arabidopsis and rice respectively. The prx genes from rice are assigned to their functional groups based on homology search against Arabidopsis protein database. Deciphering the Prx functions in rice will add novel information to the mechanism of antioxidant defense in plants. Further, the Prx also forms the part of redox signaling cascade. Here, the Prx gene family has been described for rice.Key words: antioxidant defense, chloroplast, gene family, oxidative stress, reactive oxygen speciesThe formation of free radicals and reactive oxygen species (ROS) occur in several enzymatic and non-enzymatic reactions during cellular metabolism. The accumulation of these reactive and deleterious intermediates is suppressed by antioxidant defense mechanism comprised of low molecular weight antioxidants and enzymes. In photosynthetic organisms, the defense against the damage from free radicals and oxidative stress is crucial. For instance, the ROS production occurs in photosystem II with generation of singlet oxygen (1O2) and hydrogen peroxide (H2O2),1,2 photosystem I from superoxide anion radicals (O2),3 and during photorespiration with generation of H2O2.4 ROS production may exceed under environmental stress conditions like excess light, low temperature and drought.5The antioxidant defense mechanism is activated by antioxidant metabolities and enzymes which detoxify ROS and lipid peroxides. The detoxification of ROS can occur in various cellular compartments such as chloroplasts, mitochondria, peroxisomes and cytosol.6 The enzymes like ascorbate peroxidase, catalase, glutathione peroxidase and superoxide dismutase are prominent antioxidant enzymes.6 The peroxiredoxins (Prx) emerged as new components in the antioxidant defense network of barley.7,8 Later, Prx were studied in other plants.914Prx can be classified into four different functional groups, PrxQ, 1-Cys Prx, 2-Cys Prx and Type-2 Prx.15,16 They are members of the thioredoxin fold superfamily.17,18 In this study, the prx genes found in Arabidopsis and rice genomes are been identified. The Arabidopsis genome encodes 10 prx genes classified into four functional categories, 1-Cys Prx, 2-Cys Prx, PrxQ and Type-2 Prx.13 Of these, one each of 1-Cys Prx and PrxQ, two of 2-Cys Prx (2-Cys PrxA and 2-Cys PrxB) and six Type-2 Prx (PrxA–F) are identified13 (
LocusAnnotationSynonymA*B*C*
AT1G481301-Cysteine peroxiredoxin 1 (ATPER1)1-Cys Prx21624081.36.603
AT1G60740Peroxiredoxin type 2Type-2 PrxD16217471.95.2297
AT1G65970Thioredoxin-dependent peroxidase 2 (TPX2)Type-2 PrxC16217413.95.2297
AT1G65980Thioredoxin-dependent peroxidase 1 (TPX1)Type-2 PrxB16217427.84.9977
AT1G65990Type 2 peroxiredoxin-relatedType-2 PrxA55362653.66.4368
AT3G06050Peroxiredoxin IIF (PRXIIF)Type-2 PrxF20121445.29.3905
AT3G116302-Cys Peroxiredoxin A (2CPA, 2-Cys PrxA)2-Cys PrxA26629091.77.5686
AT3G26060ATPRX Q, periredoxin QPrxQ21623677.810.0565
AT3G52960Peroxiredoxin type 2Type-2 PrxE23424684.09.572
AT5G062902-Cysteine Peroxiredoxin B (2CPB, 2-Cys PrxB)2-Cys PrxB27329779.55.414
Open in a separate window*A, amino acids; B, molecular weight; C, isoelectric point.In rice (rice.plantbiology.msu.edu/), there are 11 genomic loci which encode for Prx proteins (and33). Interestingly, a new prx gene (LOC_Os07g15670) annotated as “peroxiredoxin, putative, expressed” is identified making the tally of prx genes to eleven in rice as compared to ten in Arabidopsis (and22). The BLAST search has identified its counterpart in Arabidopsis which has been annotated as “antioxidant/oxidoreductase” (AT1G21350) in the TAIR database (www.arabidopsis.org). The rice LOC_Os07g15670 and Arabidopsis AT1G21350 share protein homology %68/78 for 236 amino acids (
ChromosomeLocus IdPutative function/AnnotationA*B*C*
1LOC_Os01g16152peroxiredoxin, putative, expressed19920873.68.2209
1LOC_Os01g24740peroxiredoxin-2E-1, chloroplast precursor, putative10711591.56.7906
1LOC_Os01g48420peroxiredoxin, putative, expressed16317290.85.6828
2LOC_Os02g09940peroxiredoxin, putative, expressed22623179.56.535
2LOC_Os02g33450peroxiredoxin, putative, expressed26228096.95.7709
4LOC_Os04g339702-Cys peroxiredoxin BAS1, chloroplast precursor, putative, expressed12213410.24.3705
6LOC_Os06g09610peroxiredoxin, putative, expressed2662892610.5097
6LOC_Os06g42000peroxiredoxin, putative, expressed23323688.39.2059
7LOC_Os07g15670peroxiredoxin, putative, expressed25327684.69.8545
7LOC_Os07g44440peroxiredoxin, putative, expressed22124232.65.3618
7LOC_Os07g44430peroxiredoxin, putative25627785.36.8544
Open in a separate window*A, amino acids; B, molecular weight; C, isoelectric point.

Table 3

Identification of rice homologs of peroxiredoxins in A. thaliana
Locus Id (Os*)Homolog (At*)NomenclatureIdentitity/Similarity (%)No. of aa* compared
LOC_Os01g16152AT3G06050Type-2 PrxF73/84201
LOC_Os01g24740AT1G65980Type-2 PrxB42/5977
LOC_Os01g48420AT1G65970Type-2 PrxC74/86162
LOC_Os02g09940AT1G60740Type-2 PrxD56/72166
LOC_Os02g33450AT5G062902-Cys Prx B74/82272
LOC_Os04g33970AT3G116302-Cys PrxA92/9688
LOC_Os06g09610AT3G26060PrxQ78/89159
LOC_Os06g42000AT3G52960Type-2 PrxE61/74240
LOC_Os07g15670AT1G21350Antioxidant68/78236
LOC_Os07g44440AT1G65990Type-2 PrxA27/4483
LOC_Os07g44430AT1G481301-Cys Prx69/83221
Open in a separate window*Os, Oryza sativa L.; At, Arabidopsis thaliana L.; aa, amino acids.The protein alignment study of Prx members in rice with the canonical Prx2-B and Prx2-E of Arabidopsis is shown in Figure 1. The Type-2 Prx proteins are characterized by the presence of catalytic cysteine (Cys) residues (Fig. 1). The alignment of rice Prx proteins shows that the Cys residue is well conserved in members like LOC_Os02g09940 (Type-2 PrxD), LOC_Os06g42000 (Type-2 Prx E), LOC_Os01g48420 (Type-2 Prx C), LOC_Os01g16152 (Type-2 Prx F), LOC_Os02g33450 (2-Cys Prx B), LOC_Os07g44440 (Type-2 Prx A), LOC_Os07g44430 (1-Cys Prx) and LOC_Os06g09610 (PrxQ) (Fig. 1). However, LOC_Os01g24740 (Type-2 PrxB) and LOC_Os04g33970 (2-Cys PrxA) which contain a chloroplast precursor do not have the catalytic Cys residues (Fig. 1). The newly identified LOC_Os07g15670 and AT1G21350 with annotations “peroxiredoxin, putative, expressed” and “antioxidant/oxidoreductase” respectively do not have catalytic Cys residues as well (Fig. 1).Open in a separate windowFigure 1Amino acid alignment of peroxiredoxins (Prx) in rice. The rice proteins are aligned with the canonical Arabidopsis Prx2-B and Prx2-E. The conserved cysteine residues are indicated by arrows on top of the alignment. Note the sequence conservation between the newly identified LOC_Os07g15670 and AT1G21350. The rice locus Ids are identified on left and amino acid positions on right. The alignment was made with ClustalX.Taken together, the results demonstrate that like Arabidopsis, the Prx constitute a small gene family in rice. However, the functional role of Prx in rice is not clearly understood. Keywords:
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