Evolutionary Implications of a Peroxidase with High Affinity for Cinnamyl Alcohols from Physcomitrium patens, a Non-Vascular Plant

Physcomitrium (Physcomitrella) patens is a bryophyte highly tolerant to different stresses, allowing survival when water supply is a limiting factor. This moss lacks a true vascular system, but it has evolved a primitive water-conducting system that contains lignin-like polyphenols. By means of a th...

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Bibliographic Details
Published in:Plants (Basel) 2021-07, Vol.10 (7), p.1476
Main Authors: Martínez-Cortés, Teresa, Pomar, Federico, Novo-Uzal, Esther
Format: Article
Language:English
Subjects:
Abiotic stress
Alcohol
Alcohols
Ammonium
Ammonium sulfate
Aquatic plants
Biosynthesis
Cell walls
Chromatography
Enzymes
Flowers & plants
Gene expression
Homology
Hydrogen peroxide
hydroxycinnamyl alcohols
Lignin
Mosses
Oxidation
Peptides
Peroxidase
Physcomitrella
Physcomitrium
plant evolution
Plants
Polyphenols
Proteins
Salt
Substrates
Vascular system
Water shortages
Water supply
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Summary:Physcomitrium (Physcomitrella) patens is a bryophyte highly tolerant to different stresses, allowing survival when water supply is a limiting factor. This moss lacks a true vascular system, but it has evolved a primitive water-conducting system that contains lignin-like polyphenols. By means of a three-step protocol, including ammonium sulfate precipitation, adsorption chromatography on phenyl Sepharose and cationic exchange chromatography on SP Sepharose, we were able to purify and further characterize a novel class III peroxidase, PpaPrx19, upregulated upon salt and H2O2 treatments. This peroxidase, of a strongly basic nature, shows surprising homology to angiosperm peroxidases related to lignification, despite the lack of true lignins in P. patens cell walls. Moreover, PpaPrx19 shows catalytic and kinetic properties typical of angiosperm peroxidases involved in oxidation of monolignols, being able to efficiently use hydroxycinnamyl alcohols as substrates. Our results pinpoint the presence in P. patens of peroxidases that fulfill the requirements to be involved in the last step of lignin biosynthesis, predating the appearance of true lignin.
ISSN:2223-7747
2223-7747
DOI:10.3390/plants10071476