Distribution, mobility, and anchoring of lignin-related oxidative enzymes in Arabidopsis secondary cell walls

Autor: Yoichiro Watanabe, Mathias Schuetz, A. Lacey Samuels, Richard Sibout, Natalie Hoffmann, Eva Yi Chou
Přispěvatelé: Department of Botany, University of British Columbia (UBC), Institut Jean-Pierre Bourgin (IJPB), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Université Paris Saclay (COmUE), Canadian Natural Sciences and Engineering Research Council (NSERC), EU/INRA Agreenskills Outgoing Fellowship, European Union's 7th Framework Programme for research, technological development and demonstration [FP7-609398], European Project: 609398,EC:FP7:PEOPLE,FP7-PEOPLE-2013-COFUND,AGREENSKILLSPLUS(2014), Chou, Eva Yi, Schuetz, Mathias, Samuels, A. Lacey
Jazyk: angličtina
Rok vydání: 2018
Předmět:
Zdroj: Journal of Experimental Botany
Journal of Experimental Botany, Oxford University Press (OUP), 2018, 69 (8), pp.1849-1859. ⟨10.1093/jxb/ery067⟩
Journal of Experimental Botany, 2018, 69 (8), pp.1849-1859. ⟨10.1093/jxb/ery067⟩
Journal of Experimental Botany 8 (69), 1849-1859. (2018)
ISSN: 0022-0957
1460-2431
DOI: 10.1093/jxb/ery067⟩
Popis: Laccases and peroxidases localize to different wall domains in Arabidopsis stems. These enzymes are tightly anchored in the secondary cell wall, providing a mechanism for spatial control of lignification.
Lignin is an important phenolic biopolymer that provides strength and rigidity to the secondary cell walls of tracheary elements, sclereids, and fibers in vascular plants. Lignin precursors, called monolignols, are synthesized in the cell and exported to the cell wall where they are polymerized into lignin by oxidative enzymes such as laccases and peroxidases. In Arabidopsis thaliana, a peroxidase (PRX64) and laccase (LAC4) are shown to localize differently within cell wall domains in interfascicular fibers: PRX64 localizes to the middle lamella whereas LAC4 localizes throughout the secondary cell wall layers. Similarly, laccases localized to, and are responsible for, the helical depositions of lignin in protoxylem tracheary elements. In addition, we tested the mobility of laccases in the cell wall using fluorescence recovery after photobleaching. mCHERRY-tagged LAC4 was immobile in secondary cell wall domains, but mobile in the primary cell wall when ectopically expressed. A small secreted red fluorescent protein (sec-mCHERRY) was engineered as a control and was found to be mobile in both the primary and secondary cell walls. Unlike sec-mCHERRY, the tight anchoring of LAC4 to secondary cell wall domains indicated that it cannot be remobilized once secreted, and this anchoring underlies the spatial control of lignification.
Databáze: OpenAIRE