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Peroxidase 4 is involved in syringyl lignin formation in Arabidopsis thaliana created by Francisco Fernández-Pérez, Tamara Vivar, Federico Pomar, María. A. Pedreño and Esther Novo-Uzal

By: Contributor(s): Material type: TextTextSeries: Journal of Plant Physiology ; Volume 175Amsterdam: Elsevier GmbH, 2015Content type:
  • text
Media type:
  • unmediated
Carrier type:
  • volume
ISSN:
  • 0176-1617
Subject(s): LOC classification:
  • QK711.2 JOU
Online resources: Abstract: Syringyl lignins result from the oxidative polymerization of sinapyl alcohol in a reaction mediated by syringyl (basic) peroxidases. Several peroxidases have been identified in the genome of Arabidopsis thaliana as close homologues to ZePrx, the best characterized basic peroxidase so far, but none of these has been directly involved in lignification. We have used a knock-out mutant of AtPrx4, the closest homologue to ZePrx, to study the involvement of this basic peroxidase in the physiology of the plant under both long- and short-day light conditions. Our results suggest that AtPrx4 is involved in cell wall lignification, especially in syringyl monomer formation. The disruption of AtPrx4 causes a decrease in syringyl units proportion, but only when light conditions are optimal. Moreover, the effect of AtPrx4 disruption is age-dependent, and it is only significant when the elongation process of the stem has ceased and lignification becomes active. In conclusion, AtPrx4 emerges as a basic peroxidase regulated by day length with an important role in lignification.
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Item type Current library Call number Vol info Status Notes Date due Barcode
Journal Article Journal Article Main Library Journal Article QK711.2 JOU (Browse shelf(Opens below)) Vol. 175 (pages86-94) Not for loan For in house use only

Syringyl lignins result from the oxidative polymerization of sinapyl alcohol in a reaction mediated by syringyl (basic) peroxidases. Several peroxidases have been identified in the genome of Arabidopsis thaliana as close homologues to ZePrx, the best characterized basic peroxidase so far, but none of these has been directly involved in lignification. We have used a knock-out mutant of AtPrx4, the closest homologue to ZePrx, to study the involvement of this basic peroxidase in the physiology of the plant under both long- and short-day light conditions. Our results suggest that AtPrx4 is involved in cell wall lignification, especially in syringyl monomer formation. The disruption of AtPrx4 causes a decrease in syringyl units proportion, but only when light conditions are optimal. Moreover, the effect of AtPrx4 disruption is age-dependent, and it is only significant when the elongation process of the stem has ceased and lignification becomes active. In conclusion, AtPrx4 emerges as a basic peroxidase regulated by day length with an important role in lignification.

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