Comparative genomics of pectinacetylesterases: Insight on function and biology

Souza, Amancio de; Pauly, Markus

doi:10.1080/15592324.2015.1055434

Cited by 13 publications

(9 citation statements)

References 18 publications

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“…Once incorporated into the cell wall, HG is further selectively modified and the pattern and degree of these modifications affect pectin hydrolysis and properties such as pH, charge and crosslinking. Pectin acetyl esterases catalyze de-acetylation and the release of acetate from the cell wall, causing changes in cell wall mechanics and developmental aberrations [ 15 , 16 ]. Pectin methyl esterases (PMEs) catalyze the specific de-methylesterification of HG, releasing methanol and protons, and creating negatively charged carboxyl groups in the process ( Figure 1 ).…”

Section: Introductionmentioning

confidence: 99%

The Multifaceted Role of Pectin Methylesterase Inhibitors (PMEIs)

Wormit

Usadel

2018

IJMS

180

126

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Plant cell walls are complex and dynamic structures that play important roles in growth and development, as well as in response to stresses. Pectin is a major polysaccharide of cell walls rich in galacturonic acid (GalA). Homogalacturonan (HG) is considered the most abundant pectic polymer in plant cell walls and is partially methylesterified at the C6 atom of galacturonic acid. Its degree (and pattern) of methylation (DM) has been shown to affect biomechanical properties of the cell wall by making pectin susceptible for enzymatic de-polymerization and enabling gel formation. Pectin methylesterases (PMEs) catalyze the removal of methyl-groups from the HG backbone and their activity is modulated by a family of proteinaceous inhibitors known as pectin methylesterase inhibitors (PMEIs). As such, the interplay between PME and PMEI can be considered as a determinant of cell adhesion, cell wall porosity and elasticity, as well as a source of signaling molecules released upon cell wall stress. This review aims to highlight recent updates in our understanding of the PMEI gene family, their regulation and structure, interaction with PMEs, as well as their function in response to stress and during development.

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Section: Introductionmentioning

confidence: 99%

The Multifaceted Role of Pectin Methylesterase Inhibitors (PMEIs)

Wormit

Usadel

2018

IJMS

180

126

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“…The 12 families in this superfamily are characterized by four conserved residues: S, G, N and H. There is also an aspartic residue that appears to be involved in the catalytic site [ 16 , 17 ]. To date, few studies have reported the biochemical properties and physiological function of PAE [ 5 , 9 , 18 – 21 ]. Furthermore, analyses of the evolution, function and structure of the PAE gene family in plants are very scarce [ 21 , 22 ].…”

Section: Introductionmentioning

confidence: 99%

“…To date, few studies have reported the biochemical properties and physiological function of PAE [ 5 , 9 , 18 – 21 ]. Furthermore, analyses of the evolution, function and structure of the PAE gene family in plants are very scarce [ 21 , 22 ]. An evolutionary history analysis of 16 pectin-related gene families from 10 diverse plant genomes showed that Physcomitrella patens , a lower plant, has fewer pectin-related gene family members compared to Arabidopsis [ 22 ].…”

Section: Introductionmentioning

confidence: 99%

“…The Physcomitrella genome was found to contain only one PAE gene while in higher plants multiple members were observed, suggesting a minimum of one ancestral PAE in the earliest land plant [ 22 ]. Another phylogenetic tree study based on PAE protein sequences from up to 35 plant species, including Arabidopsis, proposed a putative minimal set of 4 distinct PAEs in the plant for its function [ 21 ]. In addition, these authors identified three specific grass PAE clades, one of which showed a low level of conservation with the other clades of the tree, consistent with the hypothesis of a neofunctionalization of PAEs in grass.…”

Section: Introductionmentioning

confidence: 99%

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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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“…However, few studies have explored PAE physiological functions to date, or the evolution, function, and structure of the PAE gene family in plants [ 13 , 19 , 20 ]. These studies give the insight that a lower plant has fewer pectin-related gene family members compared to Arabidopsis, and only one ancestral PAE in the earliest land plant [ 11 , 20 , 21 ]. In addition, there have not been sufficient studies of the function and expression of PAEs in different plants, and the roles in plant development of these proteins remain uncertain.…”

Section: Introductionmentioning

confidence: 99%

Systematic Analysis and Functional Validation of Citrus Pectin Acetylesterases (CsPAEs) Reveals that CsPAE2 Negatively Regulates Citrus Bacterial Canker Development

Jia

Qin

et al. 2020

IJMS

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The present study was designed to serve as a comprehensive analysis of Citrus sinensis (C. sinensis) pectin acetylesterases (CsPAEs), and to assess the roles of these PAEs involved in the development of citrus bacterial canker (CBC) caused by Xanthomonas citri subsp. citri (Xcc) infection. A total of six CsPAEs were identified in the genome of C. sinensis, with these genes being unevenly distributed across chromosomes 3, 6, and 9, and the unassembled scaffolds. A subset of CsPAEs were found to be involved in responses to Xcc infection. In particular, CsPAE2 was identified to be associated with such infections, as it was upregulated in CBC-susceptible variety Wanjincheng and inversely in CBC-resistant variety Calamondin. Transgenic citrus plants overexpressing CsPAE2 were found to be more susceptible to CBC, whereas the silencing of this gene was sufficient to confer CBC resistance. Together, these findings provide evolutionary insights into and functional information about the CsPAE family. This study also suggests that CsPAE2 is a potential candidate gene that negatively contributes to bacterial canker disease and can be used to breed CBC-resistant citrus plants.

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Comparative genomics of pectinacetylesterases: Insight on function and biology

Cited by 13 publications

References 18 publications

The Multifaceted Role of Pectin Methylesterase Inhibitors (PMEIs)

The Multifaceted Role of Pectin Methylesterase Inhibitors (PMEIs)

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

Systematic Analysis and Functional Validation of Citrus Pectin Acetylesterases (CsPAEs) Reveals that CsPAE2 Negatively Regulates Citrus Bacterial Canker Development

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