Structural Motifs of Syringyl Peroxidases Are Conserved during Angiosperm Evolution

Abstract

The most distinctive variation in the monomer composition of lignins in vascular land plants is that between the two main groups of seed plants. Thus, whereas gymnosperm (softwood) lignins are typically composed of guaiacyl (G) units, angiosperm (hardwood) lignins are largely composed of similar levels of G and syringyl (S) units. However, there are some studies that suggest that certain angiosperm peroxidases are unable to oxidize sinapyl alcohol, and a coniferyl alcohol shuttle has been proposed for oxidizing S units during the biosynthesis of lignins. With this in mind, a screening of the presence of S peroxidases in angiosperms (including woody species and forages) was performed. Contrarily to what might be expected, the intercellular washing fluids from lignifying tissues of 25 woody, herbaceous, and shrub species, belonging to both monocots and dicotyledons, all showed both S peroxidase activities and basic peroxidase isoenzymes analogous, with regard the isoelectric point, to the Zinnia elegans basic peroxidase isoenzyme, the only S peroxidase that has been fully characterized. These results led to the protein database in the search for homologies between angiosperm peroxidases and a true eudicot S peroxidase, the Z. elegans peroxidase. The findings showed that certain structural motifs of S peroxidases are conserved within the first 15 million years of angiosperm history, because they are found in peroxidases from the two major lineages of flowering plants, eumagnoliids and eudicotyledons, of note being the presence of these peroxidases in Amborella and Nymphaeales, which represent the first stages of angiosperm evolution. These phylogenetic studies also suggest that guaiacyl peroxidases apparently constitute the most "evolved state" of the plant peroxidase family evolution.