000			02173nam a22003137a 4500
003			ZW-GwMSU
005			20250317142145.0
008			250317b |||||||| |||| 00| 0 eng d
022			_a0176-1617
040			_aMSU _bEnglish _cMSU _erda
050	0	0	_aQK711.2 JOU
100	1		_aFernández-Pérez, Francisco _eauthor
245	1	0	_aPeroxidase 4 is involved in syringyl lignin formation in Arabidopsis thaliana _ccreated by Francisco Fernández-Pérez, Tamara Vivar, Federico Pomar, María. A. Pedreño and Esther Novo-Uzal
264	1		_aAmsterdam: _bElsevier GmbH, _c2015.
336			_2rdacontent _atext _btxt
337			_2rdamedia _aunmediated _bn
338			_2rdacarrier _avolume _bnc
440			_aJournal of Plant Physiology _vVolume 175
520	3		_aSyringyl 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.
650			_aArabidopsis
650			_aCell wall
650			_aLignification
700	1		_aVivar, Tamara _eco-author
700	1		_aPomar, Federico _eco-author
700	1		_aPedreño, María A. _eco-author
700	1		_aNovo-Uzal, Esther _eco-author
856			_uhttps://doi.org/10.1016/j.jplph.2014.11.006
942			_2lcc _cJA
999			_c169317 _d169317