Characterization of the Arabinogalactan Protein 31 (AGP31) of Arabidopsis thaliana

Hijazi, May; Durand, Jessica; Pichereaux, Carole; Pont, Frédéric; Jamet, Élisabeth; Albenne, Cècile

doi:10.1074/jbc.m111.247874

Cited by 31 publications

(43 citation statements)

References 53 publications

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“…New fragmentation methods such as electron capture dissociation (ECD) and electron transfer dissociation (ETD) (Bond and Kohler, 2007) are also very promising. They will provide new insight into the structure of CWPs, as recently achieved for the AGP31, an A. thaliana cell wall O -glycoprotein (Hijazi et al, 2012). Finally, progresses in bioinformatics will be very helpful to characterize cell wall glycoproteins.…”

Section: Present Challenges: Overcoming Technological Bottlenecksmentioning

confidence: 85%

“…AGP31 is a multi-domain proteins having a N-terminal AGP, a central Pro-rich and a C-terminal Cys-rich domains. The combination of several MS technologies has allowed the first description of the Pro hydroxylation and O -glycosylation patterns of its Pro-rich domain (Hijazi et al, 2012). Finally, the N. tabacum NtSCP1 serine carboxypeptidase III identified in leaf intercellular fluids has been later shown to be involved in cell elongation (Delannoy et al, 2008; Bienert et al, 2012).…”

Section: Beyond Cell Wall Proteomicsmentioning

confidence: 99%

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Plant cell wall proteomics: the leadership of Arabidopsis thaliana

2013

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Plant cell wall proteins (CWPs) progressively emerged as crucial components of cell walls although present in minor amounts. Cell wall polysaccharides such as pectins, hemicelluloses, and cellulose represent more than 90% of primary cell wall mass, whereas hemicelluloses, cellulose, and lignins are the main components of lignified secondary walls. All these polymers provide mechanical properties to cell walls, participate in cell shape and prevent water loss in aerial organs. However, cell walls need to be modified and customized during plant development and in response to environmental cues, thus contributing to plant adaptation. CWPs play essential roles in all these physiological processes and particularly in the dynamics of cell walls, which requires organization and rearrangements of polysaccharides as well as cell-to-cell communication. In the last 10 years, plant cell wall proteomics has greatly contributed to a wider knowledge of CWPs. This update will deal with (i) a survey of plant cell wall proteomics studies with a focus on Arabidopsis thaliana; (ii) the main protein families identified and the still missing peptides; (iii) the persistent issue of the non-canonical CWPs; (iv) the present challenges to overcome technological bottlenecks; and (v) the perspectives beyond cell wall proteomics to understand CWP functions.

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Section: Present Challenges: Overcoming Technological Bottlenecksmentioning

confidence: 85%

Section: Beyond Cell Wall Proteomicsmentioning

confidence: 99%

Plant cell wall proteomics: the leadership of Arabidopsis thaliana

2013

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“…S2). As Pro residues of the AGP31 Pro-rich domain are known to be hydroxylated and glycosylated (Hijazi et al, 2012), it is likely that this is also the case for the conserved domain in FOCL1. However, FOCL1 and AGP31 have lower Pro content than many HRGPs and are therefore unlikely to have very high levels of posttranslational glycosylation.…”

Section: Focl1 Has Features Of Hyp-rich Cell Wall Glycoproteinsmentioning

confidence: 99%

“…Plant cuticles are anchored to cell walls by extended pectic lamellae and can be released by pectinase or cellulase treatment (Jeffree, 2006). As the Pro-rich region of FOCL1 is likely to be decorated with pectic side chains containing Gal and arabinose (Hijazi et al, 2012), it is possible that the posttranslationally modified FOCL1 protein normally interacts with pectin or cutin in the OCL where it is located (Fig. 5B).…”

Section: Role and Structure Of The Stomatal Oclmentioning

confidence: 99%

Formation of the Stomatal Outer Cuticular Ledge Requires a Guard Cell Wall Proline-Rich Protein

et al. 2017

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(K.S.); 0000-0002-6438-9188 (R.S.); 0000-0002-9703-0745 (A.J.F.); 0000-0001-9972-5156 (J.E.G.).Stomata are formed by a pair of guard cells which have thickened, elastic cell walls to withstand the large increases in turgor pressure that have to be generated to open the pore that they surround. We have characterized FOCL1, a guard cell-expressed, secreted protein with homology to Hyp-rich cell wall proteins. FOCL1-GFP localizes to the guard cell outer cuticular ledge and plants lacking FOCL1 produce stomata without a cuticular ledge. Instead the majority of stomatal pores are entirely covered over by a continuous fusion of the cuticle, and consequently plants have decreased levels of transpiration and display drought tolerance. The focl1 guard cells are larger and less able to reduce the aperture of their stomatal pore in response to closure signals suggesting that the flexibility of guard cell walls is impaired. FOCL1 is also expressed in lateral root initials where it aids lateral root emergence. We propose that FOCL1 acts in these highly specialized cells of the stomata and root to impart cell wall strength at high turgor and/or to facilitate interactions between the cell wall and the cuticle.

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“…The very high ratio of carbohydrate to protein in AGPs (i.e., 90%–10% respectively) suggests that the glycan side chains of AGPs are important in their functioning as well as their interactions with other proteins [6]. These AG polysaccharides are added by O-glycosylation, such as galactosylation in serine residues and arabinosylation/or arabinogalactosylation in hydroxyproline residues [7].…”

Section: Introductionmentioning

confidence: 99%

Cotton GalT1 Encoding a Putative Glycosyltransferase Is Involved in Regulation of Cell Wall Pectin Biosynthesis during Plant Development

Qin

Rao

et al. 2013

PLoS ONE

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Arabinogalactan proteins (AGPs), are a group of highly glycosylated proteins that are found throughout the plant kingdom. To date, glycosyltransferases that glycosylate AGP backbone have remained largely unknown. In this study, a gene (GhGalT1) encoding a putative β-1,3-galactosyltransferase (GalT) was identified in cotton. GhGalT1, belonging to CAZy GT31 family, is the type II membrane protein that contains an N-terminal transmembrane domain and a C-terminal galactosyltransferase functional domain. A subcellular localization assay demonstrated that GhGalT1 was localized in the Golgi apparatus. RT-PCR analysis revealed that GhGalT1 was expressed at relatively high levels in hypocotyls, roots, fibers and ovules. Overexpression of GhGalT1 in Arabidopsis promoted plant growth and metabolism. The transgenic seedlings had much longer primary roots, higher chlorophyll content, higher photosynthetic efficiency, the increased biomass, and the enhanced tolerance to exogenous D-arabinose and D-galactose. In addition, gas chromatography (GC) analysis of monosaccharide composition of cell wall fractions showed that pectin was changed in the transgenic plants, compared with that of wild type. Three genes (GAUT8, GAUT9 and xgd1) involved in pectin biosynthesis were dramatically up-regulated in the transgenic lines. These data suggested that GhGalT1 may be involved in regulation of pectin biosynthesis required for plant development.

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Characterization of the Arabinogalactan Protein 31 (AGP31) of Arabidopsis thaliana

Cited by 31 publications

References 53 publications

Plant cell wall proteomics: the leadership of Arabidopsis thaliana

Plant cell wall proteomics: the leadership of Arabidopsis thaliana

Formation of the Stomatal Outer Cuticular Ledge Requires a Guard Cell Wall Proline-Rich Protein

Cotton GalT1 Encoding a Putative Glycosyltransferase Is Involved in Regulation of Cell Wall Pectin Biosynthesis during Plant Development

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