Genes and Enzymes of the GT31 Family: Towards Unravelling the Function(s) of the Plant Glycosyltransferase Family Members

Egelund, Jack; Ellis, Miriam; Doblin, Monika S.; Qu, Yongmei; Bacic, Antony

doi:10.1002/9781444391015.ch7

Cited by 14 publications

(21 citation statements)

References 89 publications

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“…In addition, Irshad et al (2008) applied bioinformatic analysis to their cell wall proteomic data in Arabidopsis to identify several AGPs and Faik et al (2006) used bioinformatic analyses to identify 34 wheat and 24 rice FLAs. Bioinformatic tools have also been used to provide insight to the glycosyltransferases (GTs) involved in the assembly of AGP glycans (see Biosynthesis of Glycan Moieties) and in this way Bacic and colleagues have proposed that the CAZy GT 31 family comprise putative β-(1,3)-GalTs (Qu et al, 2008; Ellis et al, 2010; Egelund et al, 2011). …”

Section: Bioinformaticsmentioning

confidence: 99%

“…In particular, bioinformatics analysis has the potential to identify GTs likely to be involved in the biosynthesis of AG chains. Currently, sequence similarities to mammalian GTs represent one approach to identifying these enzymes, for example, as recently described by Egelund et al (2011) in which the authors adopted a bioinformatic approach to identify and systematically characterize putative GalTs from CAZy GT-family-31 responsible for synthesizing the β-(1,3)-Gal linkage. This study revealed that the Arabidopsis accessions grouped into four plant-specific clades (1, 7, 10, and 11; Table 2 ).…”

Section: Bioinformaticsmentioning

confidence: 99%

“…From studies of Arabidopsis at the molecular and biochemical level (Strasser et al, 2007; Qu et al, 2008), and from assembly of mammalian proteoglycans, it is expected that AG glycan chains that decorate AGPs are synthesized by type II membrane-bound GTs located in the Golgi apparatus. This includes members of CAZy GT-family-31 with putative β-(1,3)-GalT activity, that are suggested to be involved in synthesis of the β-(1,3)-Gal backbone in AG glycans (Qu et al, 2008; Egelund et al, 2011). …”

Section: Biosynthesis Of Glycan Moietiesmentioning

confidence: 99%

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Arabinogalactan-proteins and the research challenges for these enigmatic plant cell surface proteoglycans

Li¹,

Showalter²,

Egelund³

et al. 2012

Front. Plant Sci.

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137

143

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Arabinogalactan-proteins (AGPs) are complex glycoconjugates that are commonly found at the cell surface and in secretions of plants. Their location and diversity of structures have made them attractive targets as modulators of plant development but definitive proof of their direct role(s) in biological processes remains elusive. Here we overview the current state of knowledge on AGPs, identify key challenges impeding progress in the field and propose approaches using modern bioinformatic, (bio)chemical, cell biological, molecular and genetic techniques that could be applied to redress these gaps in our knowledge.

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Section: Bioinformaticsmentioning

confidence: 99%

Section: Bioinformaticsmentioning

confidence: 99%

Section: Biosynthesis Of Glycan Moietiesmentioning

confidence: 99%

See 1 more Smart Citation

Arabinogalactan-proteins and the research challenges for these enigmatic plant cell surface proteoglycans

Li¹,

Showalter²,

Egelund³

et al. 2012

Front. Plant Sci.

Self Cite

137

143

View full text Add to dashboard Cite

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“…This protein, GalT1, is involved in the synthesis of Lewis a epitopes in N -glycans [60]. One member of GT31 was selected in this study, At5g53340, and it belongs to clade 10 as reported in Egelund et al [61]. It must be stressed that At5g53340 is also tightly coexpressed with GAUT7 , GT4 and GT29 genes as shown in the coexpressed gene networks provided by ATTED-II.…”

Section: Resultsmentioning

confidence: 96%

Identification of Putative Rhamnogalacturonan-II Specific Glycosyltransferases in Arabidopsis Using a Combination of Bioinformatics Approaches

Voxeur

Andre²,

Breton³

et al. 2012

PLoS ONE

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Rhamnogalacturonan-II (RG-II) is a complex plant cell wall polysaccharide that is composed of an α(1,4)-linked homogalacturonan backbone substituted with four side chains. It exists in the cell wall in the form of a dimer that is cross-linked by a borate di-ester. Despite its highly complex structure, RG-II is evolutionarily conserved in the plant kingdom suggesting that this polymer has fundamental functions in the primary wall organisation. In this study, we have set up a bioinformatics strategy aimed at identifying putative glycosyltransferases (GTs) involved in RG-II biosynthesis. This strategy is based on the selection of candidate genes encoding type II membrane proteins that are tightly coexpressed in both rice and Arabidopsis with previously characterised genes encoding enzymes involved in the synthesis of RG-II and exhibiting an up-regulation upon isoxaben treatment. This study results in the final selection of 26 putative Arabidopsis GTs, including 10 sequences already classified in the CAZy database. Among these CAZy sequences, the screening protocol allowed the selection of α-galacturonosyltransferases involved in the synthesis of α4-GalA oligogalacturonides present in both homogalacturonans and RG-II, and two sialyltransferase-like sequences previously proposed to be involved in the transfer of Kdo and/or Dha on the pectic backbone of RG-II. In addition, 16 non-CAZy GT sequences were retrieved in the present study. Four of them exhibited a GT-A fold. The remaining sequences harbored a GT-B like fold and a fucosyltransferase signature. Based on homologies with glycosyltransferases of known functions, putative roles in the RG-II biosynthesis are proposed for some GT candidates.

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“…Subsequently, GalT proteins have been proven to participate in the initial steps of AGP glycosylation in both tobacco and Arabidopsis by analyzing GalT activities in vitro [23]. Particularly, At1g53290 and At3g14960, which encode plant specific β-GalTs, may be involved in the synthesis of AGPs [6], [24].…”

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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Genes and Enzymes of the GT31 Family: Towards Unravelling the Function(s) of the Plant Glycosyltransferase Family Members

Cited by 14 publications

References 89 publications

Arabinogalactan-proteins and the research challenges for these enigmatic plant cell surface proteoglycans

Arabinogalactan-proteins and the research challenges for these enigmatic plant cell surface proteoglycans

Identification of Putative Rhamnogalacturonan-II Specific Glycosyltransferases in Arabidopsis Using a Combination of Bioinformatics Approaches

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

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