A light-sensitive mutation in Arabidopsis LEW3 reveals the important role of N-glycosylation in root growth and development

© The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 68(2017), 18 vom: 02. Nov., Seite 5103-5116
1. Verfasser: Manzano, Concepción (VerfasserIn)
Weitere Verfasser: Pallero-Baena, Mercedes, Silva-Navas, J, Navarro Neila, Sara, Casimiro, Ilda, Casero, Pedro, Garcia-Mina, Jose M, Baigorri, Roberto, Rubio, Lourdes, Fernandez, Jose A, Norris, Matthew, Ding, Yiliang, Moreno-Risueno, Miguel A, Del Pozo, Juan C
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Arabidopsis N-glycosylation RNA splicing ROS peroxidase root development Arabidopsis Proteins Reactive Oxygen Species Peroxidases mehr... EC 1.11.1.- PRX34 protein, Arabidopsis EC 1.11.1.7 Mannosyltransferases EC 2.4.1.- ALG11 protein, Arabidopsis EC 2.4.1.131 PYK10 protein, Arabidopsis EC 3.2.1.21 beta-Glucosidase
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520 |a © The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com. 
520 |a Plant roots have the potential capacity to grow almost indefinitely if meristematic and lateral branching is sustained. In a genetic screen we identified an Arabidopsis mutant showing limited root growth (lrg1) due to defects in cell division and elongation in the root meristem. Positional cloning determined that lrg1 affects an alpha-1,2-mannosyltransferase gene, LEW3, involved in protein N-glycosylation. The lrg1 mutation causes a synonymous substitution that alters the correct splicing of the fourth intron in LEW3, causing a mix of wild-type and truncated protein. LRG1 RNA missplicing in roots and short root phenotypes in lrg1 are light-intensity dependent. This mutation disrupts a GC-base pair in a three-base-pair stem with a four-nucleotide loop, which seems to be necessary for correct LEW3 RNA splicing. We found that the lrg1 short root phenotype correlates with high levels of reactive oxygen species and low pH in the apoplast. Proteomic analyses of N-glycosylated proteins identified GLU23/PYK10 and PRX34 as N-glycosylation targets of LRG1 activity. The lrg1 mutation reduces the positive interaction between Arabidopsis and Serendipita indica. A prx34 mutant showed a significant reduction in root growth, which is additive to lrg1. Taken together our work highlights the important role of N-glycosylation in root growth and development 
650 4 |a Journal Article 
650 4 |a Arabidopsis 
650 4 |a N-glycosylation 
650 4 |a RNA splicing 
650 4 |a ROS 
650 4 |a peroxidase 
650 4 |a root development 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Reactive Oxygen Species  |2 NLM 
650 7 |a Peroxidases  |2 NLM 
650 7 |a EC 1.11.1.-  |2 NLM 
650 7 |a PRX34 protein, Arabidopsis  |2 NLM 
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650 7 |a EC 3.2.1.21  |2 NLM 
700 1 |a Pallero-Baena, Mercedes  |e verfasserin  |4 aut 
700 1 |a Silva-Navas, J  |e verfasserin  |4 aut 
700 1 |a Navarro Neila, Sara  |e verfasserin  |4 aut 
700 1 |a Casimiro, Ilda  |e verfasserin  |4 aut 
700 1 |a Casero, Pedro  |e verfasserin  |4 aut 
700 1 |a Garcia-Mina, Jose M  |e verfasserin  |4 aut 
700 1 |a Baigorri, Roberto  |e verfasserin  |4 aut 
700 1 |a Rubio, Lourdes  |e verfasserin  |4 aut 
700 1 |a Fernandez, Jose A  |e verfasserin  |4 aut 
700 1 |a Norris, Matthew  |e verfasserin  |4 aut 
700 1 |a Ding, Yiliang  |e verfasserin  |4 aut 
700 1 |a Moreno-Risueno, Miguel A  |e verfasserin  |4 aut 
700 1 |a Del Pozo, Juan C  |e verfasserin  |4 aut 
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