The class III peroxidase multigenic family in rice and its evolution in land plants☆☆☆

Passardi, Filippo; Longet, David; Penel, Claude; Dunand, Christophe

doi:10.1016/j.phytochem.2004.06.023

Cited by 347 publications

(352 citation statements)

References 56 publications

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“…Class III peroxidase encoding sequences and peroxidase activity are both absent from the green alga Chlamydomonas reinhardtii (Passardi et al, 2004). On the contrary, in various Chara species, guaiacol oxidation in the presence of H 2 O 2 , specific to class III peroxidase activity (Greppin et al, 1986), can be detected (data not shown).…”

Section: Modelization Of the Number Of Class III Isoforms Evolutionmentioning

confidence: 87%

“…We have then used AtPrx42 and OsPrx73, two sequences potentially related to an ancestral sequence (Passardi et al, 2004), for a second, more specific approach by scanning numerous public sources of plant ESTs and genome sequences in order to obtain a large collection of peroxidase-encoding sequences. For rare species, a tBLASTn was first performed against the NCBI whole database using limited queries for the date and for the organism.…”

Section: Construction Of the Databasementioning

confidence: 99%

“…Plant peroxidases are an example of a multigenic family whose number of members increased since the conquering of land by plants due to constant evolution. The Arabidopsis genome contains 73 genes encoding a peroxidase (Tognolli et al, 2002) and rice contains 138 (Passardi et al, 2004). The homology between paralogs in a plant ranges from 30% to 100%, but very close orthologs exist, even between evolutionarily distant plants.…”

Section: Introductionmentioning

confidence: 99%

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PeroxiBase: A class III plant peroxidase database

et al. 2006

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Class III plant peroxidases (EC 1.11.1.7), which are encoded by multigenic families in land plants, are involved in several important physiological and developmental processes. Their varied functions are not yet clearly determined, but their characterization will certainly lead to a better understanding of plant growth, differentiation and interaction with the environment, and hence to many exciting applications. Since there is currently no central database for plant peroxidase sequences and many plant sequences are not deposited in the EMBL/GenBank/DDBJ repository or the UniProt KnowledgeBase, this prevents researchers from easily accessing all peroxidase sequences. Furthermore, gene expression data are poorly covered and annotations are inconsistent. In this rapidly moving field, there is a need for continual updating and correction of the peroxidase superfamily in plants. Moreover, consolidating information about peroxidases will allow for comparison of peroxidases between species and thus significantly help making correlations of function, structure or phylogeny. We report a new database (PeroxiBase) accessible through a web server (http://peroxidase.isb-sib.ch) with specific tools dedicated to facilitate query, classification and submission of peroxidase sequences. Recent developments in the field of plant peroxidase are also mentioned.

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Section: Modelization Of the Number Of Class III Isoforms Evolutionmentioning

confidence: 87%

Section: Construction Of the Databasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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PeroxiBase: A class III plant peroxidase database

et al. 2006

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“…In isolated segments of maize modulated ROS yields H2O2, which boosts leaf expansion (Rodriguez et al, 2002). Moreover, in germinating pea seeds high amount of O2 − deposits at radicle expansion stage , which validates the role of O2 − in stimulating cell elongation (Passardi et al, 2004;Barba-Espin et al, 2011). Apart from their deleterious effects, ROS play a pivotal role in the signal transduction system of seed.…”

Section: Reactive Oxygen Species (Ros) and Signalingmentioning

confidence: 67%

Genomics: A Hallmark to Monitor Molecular and Biochemical Processes Leading Toward a Better Perceptive of Seed Aging and ex-situ Conservation

Ahmad¹,

Shah²,

Rehman³

et al. 2017

Current Issues in Molecular Biology

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Abbreviations:AFLP, amplified fragment length polymorphism AGO, argonaute miRNA, micro RNA NGS, next generation sequencing PCD, programmed cell death PIMT, protein L-isoaspartyl methyltransferase PRC2, Polycomb repressive complex 2 RAPD, random amplification of polymorphic DNA ROS, reactive oxygen species SSR, simple sequence repeat TUNEL, terminal deoxynucleotide transferasemediated dUTP nick-end labeling qRT-PCR, quantitative reverse transcriptional polymerase chain reaction Abstract For human food security, the preservation of 7.4 million ex-situ germplasm is a global priority. However, ex situ-conserved seeds are subject to aging, which reduces their viability and ultimately results in the loss of valuable genetic material over long periods. Recent progress in seed biology and genomics has revealed new opportunities to improve the long-term storage of ex-situ seed germplasm. This review summarizes the recent improvements in seed physiology and genomics, with the intention of developing genomic tools for evaluating seed aging. Several lines of seed biology research have shown promise in retrieving viability signal from various stages of seed germination. We conclude that seed aging is associated with mitochondrial alteration and programmed cell death, DNA and enzyme repair, anti-oxidative genes, telomere length, and epigenetic regulation. Clearly, opportunities exist for observing seed aging for developing genomic tools to increment the traditional germination test for effective conservation of ex-situ germplasm.

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“…In fact, it is known that protein structure, amino acid residues and protein size are conserved in all class III peroxidases [5,35]. CavPrx showed a "three intron" structure that is a common feature of the most of class III peroxidases in rice and Arabidopsis [2,7]. This is the first class III peroxidase isolated in C. avellana and Real Time analysis showed that it is expressed in the styles, with a peak of expression in mature styles; in addition its level of expression increased significantly in styles pollinated with compatible pollen.…”

Section: Discussionmentioning

confidence: 99%

Isolation of a gene encoding for a class III peroxidase in female flower of Corylus avellana L.

et al. 2012

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Hazelnut is a monoecius species characterized by mid-winter blooming and sporophytic incompatibility. The molecular mechanisms at the basis of the female flower development and of the pollen-stigma interaction are little known, although pollination in this species is a critical factor to ensure good yield. Differential Display technique was used to study genes expressed during the female flower development, comparing styles before emergence from the bud and styles at full bloom. The full-length cDNA clone, designated CavPrx (Corylus avellana peroxidase) and isolated in mature styles, was characterized as a sequence encoding for a 330 amino acids protein, containing all the conserved features of class III peroxidases. CavPrx resulted expressed only in styles, with a peak in mature styles pollinated with compatible pollen. Class III peroxidases are expressed in several different plant tissue types and are involved in a broad spectrum of physiological processes. Until now, four peroxidases expressed in the stigma were identified in Arabidopsis thaliana and Senecio squalidus: they were assumed to be possibly involved in pollen-pistil interaction, pollen tube penetration/growth and/or in defence against pathogens. CavPrx is the first gene for a floral peroxidase isolated in hazelnut and its expression pattern suggests a possible role in the pollination process.

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The class III peroxidase multigenic family in rice and its evolution in land plants☆☆☆

Cited by 347 publications

References 56 publications

PeroxiBase: A class III plant peroxidase database

PeroxiBase: A class III plant peroxidase database

Genomics: A Hallmark to Monitor Molecular and Biochemical Processes Leading Toward a Better Perceptive of Seed Aging and ex-situ Conservation

Isolation of a gene encoding for a class III peroxidase in female flower of Corylus avellana L.

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