Distribution of pectic epitopes in cell walls of the sugar beet root

Guillemin, Florence; Guillon, Fabienne; Bonnin, Estelle; Devaux, Marie-Françoise; Chevalier, Thérèse M.; Knox, John; Liners, Françoise; Thibault, Jean‐François

doi:10.1007/s00425-005-1535-3

Cited by 60 publications

(46 citation statements)

References 53 publications

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“…methylesterificiation (i.e. high negative charge; Guillemin et al, 2005). This is in keeping with the contention that Al bound strongly in the cell wall limits cell elongation and root growth (Ma et al, 2004).…”

Section: Spatial Distribution Of Al In Rootssupporting

confidence: 65%

Identification of the Primary Lesion of Toxic Aluminum in Plant Roots

et al. 2015

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Despite the rhizotoxicity of aluminum (Al) being identified over 100 years ago, there is still no consensus regarding the mechanisms whereby root elongation rate is initially reduced in the approximately 40% of arable soils worldwide that are acidic. We used high-resolution kinematic analyses, molecular biology, rheology, and advanced imaging techniques to examine soybean (Glycine max) roots exposed to Al. Using this multidisciplinary approach, we have conclusively shown that the primary lesion of Al is apoplastic. In particular, it was found that 75 µm Al reduced root growth after only 5 min (or 30 min at 30 µm Al), with Al being toxic by binding to the walls of outer cells, which directly inhibited their loosening in the elongation zone. An alteration in the biosynthesis and distribution of ethylene and auxin was a second, slower effect, causing both a transient decrease in the rate of cell elongation after 1.5 h but also a longer term gradual reduction in the length of the elongation zone. These findings show the importance of focusing on traits related to cell wall composition as well as mechanisms involved in wall loosening to overcome the deleterious effects of soluble Al.

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Section: Spatial Distribution Of Al In Rootssupporting

confidence: 65%

Identification of the Primary Lesion of Toxic Aluminum in Plant Roots

et al. 2015

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“…Several antibodies exhibiting diVerent speciWcities to HG with respect to their degree and pattern of methyl-esteriWcation (Liners et al 1989(Liners et al , 1992VandenBosch et al 1989;Knox et al 1990;Willats et al 1999aWillats et al , 2001b and to arabinan and (arabino)-galactan side-chains (Jones et al 1997;Willats et al 1998;Verhertbruggen et al 2009) have been developed and used to probe pectin structural domains in situ. They revealed variation in pectin structures according to cell types and stages of cellular development and provide new insight into the functional role of the diVerent pectin domains in the context of cell wall biology (Liners et al 1994;Guglielmino et al 1997;Bush and McCann 1999;Willats et al 1999bWillats et al , 2001bErmel et al 2000;His et al 2001;McCartney et al 2003;Guillemin et al 2005;Guillon et al 2008;Verhertbruggen et al 2009). Up to now, no well-characterized antibodies against the RG-I backbone have been produced and information on their occurrence in relation to cell status, development or cell types is sparse.…”

Section: Introductionmentioning

confidence: 95%

Monoclonal antibodies to rhamnogalacturonan I backbone

Ralet

Tranquet

Poulain

et al. 2010

Planta

117

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Monoclonal antibodies were raised against rhamnogalacturonan I backbone, a pectin domain, using Arabidopsis thaliana seed mucilage-derived rhamnogalacturonan I oligosaccharides--BSA conjugates. Two monoclonal antibodies, designated INRA-RU1 and INRA-RU2, selected for further characterization, were specific for the backbone of rhamnogalacturonan I, displaying no binding activity against the other pectin domains i.e. homogalacturonans, galactans or arabinans. A range of oligosaccharides was prepared by enzymatic digestion of rhamnogalacturonan I isolated from Arabidopsis thaliana seed mucilage and from sugar beet pectin, purified by low-pressure chromatography and characterized by high-performance anion-exchange chromatography and mass spectrometry. These rhamnogalacturonan I oligomers were used to characterize the binding site of the two monoclonal antibodies by competitive inhibition. Both INRA-RU1 and INRA-RU2 showed maximal binding to the [-->2)-alpha-L-rhamnosep-(1-->4)-alpha-D-galacturonic acid p-(1-->](7) structural motif but differed in their minimum binding requirement. INRA-RU2 required at least two disaccharide (rhamnose-galacturonic acid) repeats for the antibody to bind, while INRA-RU1 required a minimum of six disaccharide repeats. Furthermore, the binding capacity of INRA-RU1 decreased steeply as the number of disaccharide repeats go beyond seven. Each of these antibodies reacted with hairy regions isolated from sugar beet pectin. Immunofluorescence microscopy indicated that both antibodies can be readily used to detect rhamnogalacturonan I epitopes in various cell wall samples.

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“…Sugar beet root sample embedded in resin (LRW) was available from previous study (Guillemin et al 2005).…”

Section: Biological Materialsmentioning

confidence: 99%

Investigation of ferulate deposition in endosperm cell walls of mature and developing wheat grains by using a polyclonal antibody

Philippe

Tranquet

Utille

et al. 2006

Planta

Self Cite

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A polyclonal antibody has been raised against ferulic acid ester linked to arabinoxylans (AX). 5-O-feruloyl-alpha-L-arabinofuranosyl(1-->4)-beta-D-xylopyranosyl was obtained by chemical synthesis, and was coupled to bovine serum albumin for the immunization of rabbit. The polyclonal antibody designated 5-O-Fer-Ara was highly specific for 5-O-(trans-feruloyl)-L-arabinose (5-O-Fer-Ara) structure that is a structural feature of cell wall AX of plants belonging to the family of Gramineae. The antibody has been used to study the location and deposition of feruloylated AX in walls of aleurone and starchy endosperm of wheat grain. 5-O-Fer-Ara began to accumulate early in aleurone cell wall development (beginning of grain filling, 13 days after anthesis, DAA) and continued to accumulate until the aleurone cells were firmly fixed between the starchy endosperm and the nucelus epidermis (19 DAA). From 26 DAA to maturity, the aleurone cell walls changed little in appearance. The concentration of 5-O-Fer-Ara is high in both peri- and anticlinal aleurone cell walls with the highest accumulation of 5-O-Fer-Ara at the cell junctions at the seed coat interface. The situation is quite different in the starchy endosperm: whatever the stage of development, a low amount of 5-O-Fer-Ara epitope was detected. Contrary to what was observed for aleurone cell walls, no peak of accumulation of feruloylated AX was noticed between 13 and 19 DAA. Visualization of labelled Golgi vesicles suggested that the feruloylation of AX is intracellular. The distribution of (5-O-Fer-Ara) epitope is further discussed in relation to the role of ferulic acid and its dehydrodimers in cell wall structure and tissue organization of wheat grain.

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Distribution of pectic epitopes in cell walls of the sugar beet root

Cited by 60 publications

References 53 publications

Identification of the Primary Lesion of Toxic Aluminum in Plant Roots

Identification of the Primary Lesion of Toxic Aluminum in Plant Roots

Monoclonal antibodies to rhamnogalacturonan I backbone

Investigation of ferulate deposition in endosperm cell walls of mature and developing wheat grains by using a polyclonal antibody

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