Basic peroxidases in cell walls of plants belonging to the Asteraceae family

Barceló, A. Ros; Aznar-Asensio, Ginés J.

doi:10.1078/0176-1617-00619

Cited by 9 publications

(3 citation statements)

References 27 publications

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“…It is worth noting that the affinity of this strongly basic peroxidase for cinnamyl alcohols and aldehydes is similar to that shown by the preceding enzymes in the lignin biosynthetic pathway (microsomal 5‐hydroxylases and cinnamyl alcohol dehydrogenase), which also use cinnamyl alcohols and aldehydes as substrates [12], indicating that the one‐way highway of lignin macromolecule construction has no metabolic ‘potholes’ into which the lignin building blocks might accumulate. This fact suggests a high degree of metabolic plasticity for this basic peroxidase, which has been widely conserved during the evolution of vascular plants [13], making it one of the driving forces in the evolution of plant lignin heterogeneity.…”

Section: Introductionmentioning

confidence: 99%

H₂O₂ generation during the auto‐oxidation of coniferyl alcohol drives the oxidase activity of a highly conserved class III peroxidase involved in lignin biosynthesis

et al. 2002

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Characterization of ligni¢ed Zinnia elegans hypocotyls by both alkaline nitrobenzene oxidation and thioacidolysis reveals that coniferyl alcohol units are mainly found as part of 4-O-linked end groups and aryl-glycerol-L L-aryl ether (L L-O-4) structures. Z. elegans hypocotyls also contain a basic peroxidase (EC 1.11.1.7) capable of oxidizing coniferyl alcohol in the absence of H 2 O 2 . Results showed that the oxidase activity of the Z. elegans basic peroxidase is stimulated by superoxide dismutase, and inhibited by catalase and anaerobic conditions. Results also showed that the oxidase activity of this peroxidase is due to an evolutionarily gained optimal adaptation of the enzyme to the W WM H 2 O 2 concentrations generated during the auto-oxidation of coniferyl alcohol, the stoichiometry of the chemical reaction (mol coniferyl alcohol auto-oxidized/mol H 2 O 2 formed) being 0.496. These results therefore suggest that the H 2 O 2 generated during the auto-oxidation of coniferyl alcohol is the main factor that drives the unusual oxidase activity of this highly conserved lignin-synthesizing class III peroxidase.

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Section: Introductionmentioning

confidence: 99%

H₂O₂ generation during the auto‐oxidation of coniferyl alcohol drives the oxidase activity of a highly conserved class III peroxidase involved in lignin biosynthesis

et al. 2002

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“…Several reports suggest that both acidic and basic peroxidases are involved in lignin synthesis depending on plant species (Ostegaard et al 2000;Ros Barceló and Aznar-Asensio 2002). However, it has been also suggested that both cationic and anionic peroxidases are required for correct lignification of CW (Mä der et al 1986).…”

Section: Discussionmentioning

confidence: 96%

Cadmium induces premature xylogenesis in barley roots

et al. 2006

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The effect of Cd on H 2 O 2 production, peroxidase (POD) activity and root hair formation were analyzed in barley root. Cd causes a strong H 2 O 2 burst in the root region 0-6 mm behind the root tip. POD activity was activated in root tip and raised toward the root base in Cd treated roots. In situ analyses showed that both elevated H 2 O 2 production and POD activity are localized in the early metaxylem vascular bundles. Cd induces root hair formation in the region 2 to 4 mm behind the root tip that was not detected in control roots. These results suggest that Cd-induced root growth inhibition is at least partially the consequence of Cd-stimulated premature root development involving xylogenesis and root hair formation, which is correlated with shortening of root elongation zone and therefore with root growth reduction.

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“…Although from the high isoelectric point (about 10.2-10.5), and from the electrostatic surface properties (Fig. 10), one may expect that ZePrxs are firmly bound to the pectin matrix of the primary plant cell wall (Ferrer et al 1992), this is not apparently the case, since ZePrxs show an high mobility in the cell wall intercellular spaces, the proteins being almost all recovered in the unbound cell wall protein fraction (Ros Barceló and Aznar-Asensio 2002). Pectin-basic protein interactions may be attenuated by coating basic proteins with glycans, the best example being extensin (Cassab and Varner 1988), and, in this way, glycans of ZePrxs might reduce the electrostatic interactions with pectins, allowing ZePrxs to move freely in the cell wall matrix, and reach the secondary cell wall layer where, after starting in primary cell walls, progressively finalizes lignin deposition (Smith et al 1994).…”

Section: Inhibitormentioning

confidence: 95%

Post-translational modifications of the basic peroxidase isoenzyme from Zinnia elegans

et al. 2007

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The major basic peroxidase (ZePrx) from Zinnia elegans suspension cell cultures was purified and cloned. The purification resolved ZePrxs in two isoforms (ZePrx33.44 and ZePrx34.70), whose co-translational and post-translational modifications are characterized. Based on the N-terminal sequence obtained by Edman degradation of mature ZePxs, it may be expected that the immature polypeptides of ZePrxs contain a signal peptide (N-terminal pro-peptide) of 30 amino acids, which directs the polypeptide chains to the ER membrane. These immature polypeptides are co-translationally processed by proteolytic cleavage, and modeling studies of digestions suggested that the processing of the N-terminal pro-peptide of ZePrxs is performed by a peptidase from the SB clan (S8 family, subfamily A) of serine-type proteases. When the post-translational modifications of ZePrxs were characterized by trypsin digestion, and tryptic peptides were analyzed by reverse phase nano liquid chromatography (RP-nanoLC) coupled to MALDI-TOF MS, it was seen that, despite the presence in the primary structure of the protein of several (disulphide bridges, N-glycosylation, phosphorylation and N-myristoylation) potential post-translational modification sites, ZePrxs are only post-translationated modified by the formation of N-terminal pyroglutamate residues, disulphide bridges and N-glycosylation. Glycans of ZePrxs belong to three main types and conduce to the existence of at least ten different molecular isoforms. The first glycans belong to both low and high mannose-type glycans, with the growing structure Man(3-9)(GlcNAc)(2). Low mannose-type glycans, Man(3-4)(GlcNAc)(2), coexist with the truncated (paucimannosidic-type) glycan, Man(3)Xyl(1)Fuc(1)(GlcNAc)(2), in the G(3) and G(4 )sub-isoforms of ZePrx33.44. In ZePrx34.70, on the other hand, the complex-type biantennary glycan, Man(3)Xyl(1)Fuc(3)(GlcNAc)(5), and the truncated (paucimannosidic-type) glycan, Man(3)Xyl(1)Fuc(1)(GlcNAc)(2), appear to fill the two putative sites for N-glycosylation. Since the two N-glycosylation sites in ZePrxs are located in an immediately upstream loop region of helix F'' (close to the proximal histidine) and in helix F'' itself, and are flanked by positive-charged amino acids that produce an unusual positive-net surface electrostatic charge pattern, it may be expected that glycans not only affect reaction dynamics but may well participate in protein/cell wall interactions. These results emphasize the complexity of the ZePrx proteome and the difficulties involved in establishing any fine structure-function relationship.

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Basic peroxidases in cell walls of plants belonging to the Asteraceae family

Cited by 9 publications

References 27 publications

H₂O₂ generation during the auto‐oxidation of coniferyl alcohol drives the oxidase activity of a highly conserved class III peroxidase involved in lignin biosynthesis

H₂O₂ generation during the auto‐oxidation of coniferyl alcohol drives the oxidase activity of a highly conserved class III peroxidase involved in lignin biosynthesis

Cadmium induces premature xylogenesis in barley roots

Post-translational modifications of the basic peroxidase isoenzyme from Zinnia elegans

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Basic peroxidases in cell walls of plants belonging to the Asteraceae family

Cited by 9 publications

References 27 publications

H2O2 generation during the auto‐oxidation of coniferyl alcohol drives the oxidase activity of a highly conserved class III peroxidase involved in lignin biosynthesis

H2O2 generation during the auto‐oxidation of coniferyl alcohol drives the oxidase activity of a highly conserved class III peroxidase involved in lignin biosynthesis

Cadmium induces premature xylogenesis in barley roots

Post-translational modifications of the basic peroxidase isoenzyme from Zinnia elegans

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Product

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H₂O₂ generation during the auto‐oxidation of coniferyl alcohol drives the oxidase activity of a highly conserved class III peroxidase involved in lignin biosynthesis

H₂O₂ generation during the auto‐oxidation of coniferyl alcohol drives the oxidase activity of a highly conserved class III peroxidase involved in lignin biosynthesis