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Artículo

Low sugar is not always good: Impact of specific o-glycan defects on tip growth in arabidopsis

Velásquez, Silvia MelinaIcon ; Marzol, ElianaIcon ; Borassi, CeciliaIcon ; Pol-Fachin, Laercio; Ricardi, Martiniano MaríaIcon ; Mangano, SilvinaIcon ; Denita Juárez, Silvina PaolaIcon ; Salgado Salter, Juan DavidIcon ; Gloazzo Dorosz, Javier AnselmoIcon ; Marcus, Susan E.; Knox, J. Paul; Dinneny, Jose R.; Iusem, Norberto DanielIcon ; Verli, Hugo; Estevez, Jose ManuelIcon
Fecha de publicación: 05/2015
Editorial: American Society of Plant Biologist
Revista: Plant Physiology
ISSN: 0032-0889
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Bioquímica y Biología Molecular

Resumen

Hydroxyproline (Hyp)-rich O-glycoproteins (HRGPs) comprises several groups of O-glycoproteins including extensins (EXTs), ultimately secreted into plant cell walls. The latter are shaped by several posttranslational modifications (PTMs), mainly hydroxylation of proline residues into hydroxyproline (Hyp) and further O-glycosylation on Hyp and Serine (Ser) (Fig. S1A). EXTs contain several Ser-(Hyp)4 repeats usually O-glycosylated with chains of up to 4-5 linear arabinosyl units on each Hyp (Velasquez et al., 2011; Ogawa-Ohnishi et al., 2013) and mono-galactosylated on Ser residues (Saito et al., 2014). In this context, three groups of arabinosyltransferases (AraTs), HPAT1-HPAT3 (classified as GT8 in the Carbohydrate Active enZymes database [CAZy]), RRA1-RRA3 and XEG113 (GT77 family) have recently been implicated in the sequential addition of the innermost three L-Ara residues (Egelund et al., 2007; Ogawa-Ohnishi et al., 2013). In addition, one novel peptidyl-Ser galactosyltransferase named SERGT1 has been reported to add a single -Galp residue to each Ser residue in Ser-(Hyp)4 motifs of EXTs, thus belonging to a new family within CAZy (Table S1). Finally, glycosylated EXTs are possibly crosslinked by putative type-III peroxidases (PERs) at the Tyr residues by forming EXT linkages (Cannon et al., 2008) able to build a three-dimensional network likely to interact with other cell wall components like pectins (Cannon et al., 2008). Here, by using appropriate mutants of several known enzymes of the O-glycosylation pathway of HRGPs, we addressed to what extent each single defect on the O-glycosylation machinery impacts on root hair tip growth.
Palabras clave: O-GLYCANS , ROOT HAIR , TIP GROWTH , ARABIDOPSIS
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)
Identificadores
URI: http://hdl.handle.net/11336/182727
URL: https://academic.oup.com/plphys/article/168/3/808/6113727
DOI: https://doi.org/10.1104/pp.114.255521
Colecciones
Articulos(IFIBYNE)
Articulos de INST.DE FISIOL., BIOL.MOLECULAR Y NEUROCIENCIAS
Citación
Velásquez, Silvia Melina; Marzol, Eliana; Borassi, Cecilia; Pol-Fachin, Laercio; Ricardi, Martiniano María; et al.; Low sugar is not always good: Impact of specific o-glycan defects on tip growth in arabidopsis; American Society of Plant Biologist; Plant Physiology; 168; 3; 5-2015; 808-813
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