Expression of mung bean pectin acetyl esterase in potato tubers: effect on acetylation of cell wall polymers and tuber mechanical properties

Orfila, Caroline; Degan, Florence Dal; Jørgensen, Bodil; Scheller, Henrik Vibe; Ray, Peter M.; Ulvskov, Peter

doi:10.1007/s00425-012-1596-z

Cited by 48 publications

(43 citation statements)

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“…The degree of acetylation can be regulated by pectin acetylesterase (E.C. 3.1.1.6; PAE) which cleave the acetylester bond from pectin [5, 9]. Plant PAEs belong to family CE13 of carbohydrate esterases in the CAZy database [10].…”

Section: Introductionmentioning

confidence: 99%

Plant pectin acetylesterase structure and function: new insights from bioinformatic analysis

2017

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BackgroundPectins are plant cell wall polysaccharides that can be acetylated on C2 and/or C3 of galacturonic acid residues. The degree of acetylation of pectin can be modulated by pectin acetylesterase (EC 3.1.1.6, PAE). The function and structure of plant PAEs remain poorly understood and the role of the fine-tuning of pectin acetylation on cell wall properties has not yet been elucidated.ResultsIn the present study, a bioinformatic approach was used on 72 plant PAEs from 16 species among 611 plant PAEs available in plant genomic databases. An overview of plant PAE proteins, particularly Arabidopsis thaliana PAEs, based on phylogeny analysis, protein motif identification and modeled 3D structure is presented. A phylogenetic tree analysis using protein sequences clustered the plant PAEs into five clades. AtPAEs clustered in four clades in the plant kingdom PAE tree while they formed three clades when a phylogenetic tree was performed only on Arabidopsis proteins, due to isoform AtPAE9. Primitive plants that display a smaller number of PAEs clustered into two clades, while in higher plants, the presence of multiple members of PAE genes indicated a diversification of AtPAEs. 3D homology modeling of AtPAE8 from clade 2 with a human Notum protein showed an α/β hydrolase structure with the hallmark Ser-His-Asp of the active site. A 3D model of AtPAE4 from clade 1 and AtPAE10 from clade 3 showed a similar shape suggesting that the diversification of AtPAEs is unlikely to arise from the shape of the protein. Primary structure prediction analysis of AtPAEs showed a specific motif characteristic of each clade and identified one major group of AtPAEs with a signal peptide and one group without a signal peptide. A multiple sequence alignment of the putative plant PAEs revealed consensus sequences with important putative catalytic residues: Ser, Asp, His and a pectin binding site. Data mining of gene expression profiles of AtPAE revealed that genes from clade 2 including AtPAE7, AtPAE8 and AtPAE11, which are duplicated genes, are highly expressed during plant growth and development while AtPAEs without a signal peptide, including AtPAE2 and AtPAE4, are more regulated in response to plant environmental conditions.ConclusionBioinformatic analysis of plant, and particularly Arabidopsis, AtPAEs provides novel insights, including new motifs that could play a role in pectin binding and catalytic sites. The diversification of AtPAEs is likely to be related to neofunctionalization of some AtPAE genes.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-017-3833-0) contains supplementary material, which is available to authorized users.

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Section: Introductionmentioning

confidence: 99%

Plant pectin acetylesterase structure and function: new insights from bioinformatic analysis

2017

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“…Briefly, the pectin macromolecule used in this study contains long linear segments of alternating highly acetylated and partially methyl-esterified α-D- galacturonic acid and L-rhamnose (rhamnogalacturonan I–RG-I) essentially devoid of linear α-D- galacturonic acid (homogalacturonan—HG). Potato RG-I is documented to have a high degree of acetylation (DA) and is found to be in the range of DA 54.7 [13]. The RG-I, produced by the procedure described in Byg et al [12] was further treated with PG-III (CAE 46195, exo-polygalacturonase, Novozymes, Denmark) until the galacturonic acid:rhamnose (GalA:Rha) ratio was 1.08.…”

Section: Methodsmentioning

confidence: 99%

Rhamnogalacturonan-I Based Microcapsules for Targeted Drug Release

et al. 2016

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Drug targeting to the colon via the oral administration route for local treatment of e.g. inflammatory bowel disease and colonic cancer has several advantages such as needle-free administration and low infection risk. A new source for delivery is plant-polysaccharide based delivery platforms such as Rhamnogalacturonan-I (RG-I). In the gastro-intestinal tract the RG-I is only degraded by the action of the colonic microflora. For assessment of potential drug delivery properties, RG-I based microcapsules (~1 μm in diameter) were prepared by an interfacial poly-addition reaction. The cross-linked capsules were loaded with a fluorescent dye (model drug). The capsules showed negligible and very little in vitro release when subjected to media simulating gastric and intestinal fluids, respectively. However, upon exposure to a cocktail of commercial RG-I cleaving enzymes, ~ 9 times higher release was observed, demonstrating that the capsules can be opened by enzymatic degradation. The combined results suggest a potential platform for targeted drug delivery in the terminal gastro-intestinal tract.

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“…While the biological role of these enzymes is not fully established, mutants lacking specific PAEs exhibit changes in cell wall rigidity and display plant developmental aberrations. [4][5][6] Complete elucidation of PAE gene function and biochemistry has not yet been achieved, mostly due to genetic redundancy and difficulties in determining the exact substrate specificity. Due to its gelling and thickening properties pectins are extensively used by the food industry.…”

Section: Comparative Genomics Of Pectinacetylesterases: Insight On Fumentioning

confidence: 99%

“…4 An ortholog of the Arabidopsis PAE8 from mung bean (Vigna unguiculata) was overexpressed in potato, resulting in decreased pectin acetylation, stiffer tubers and a stronger wall matrix. 6 A poplar ortholog of the Arabidopsis PAE7, when overexpressed in tobacco, produced profound developmental alterations in pollen grains and floral structures. 5 These results demonstrate the significance of the PAE genes for plant developmental processes.…”

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confidence: 99%