ArticlePlant physiology2017
Combined Experimental and Computational Approaches Reveal Distinct pH Dependence of Pectin Methylesterase Inhibitors.
Article in Plant physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 63 citations in OpenAlex.
- Endogenous RALF peptide function is required for powdery mildew host colonization.The New phytologist · 2026Article
- FcMAPK4-phosphorylated FcNOR activates FcERF5 to promote fig fruit softening through activation of FcPG12 expression.Journal of integrative plant biology · 2026Article
- Maize Anther Development Involves Translated Open Reading Frames From 3' Untranslated Regions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Dual role of pectin methyl esterase activity in the regulation of plant cell wall biophysical properties.Frontiers in plant science · 2025Article
- A 3-component module maintains sepal flatness in Arabidopsis.Current biology : CB · 2024Article
- Homogalacturonan Pectins Tuned as an Effect of Susceptible rbohD, Col-0-Reactions, and Resistance rbohF-, rbohD/F-Reactions to TuMV.International journal of molecular sciences · 2024Article
- The plant cell wall-dynamic, strong, and adaptable-is a natural shapeshifter.The Plant cell · 2024Review
- Expansin SlExp1 and endoglucanase SlCel2 synergistically promote fruit softening and cell wall disassembly in tomato.The Plant cell · 2024Article
- Genome-wide identification and characterization of pectin methylesterase inhibitor gene family members related to abiotic stresses in watermelon.Frontiers in plant science · 2024Article
- Auxin as an architect of the pectin matrix.Journal of experimental botany · 2023Review
- Insights into cell wall changes during fruit softening from transgenic and naturally occurring mutants.Plant physiology · 2023Review
- AtMYB50 regulates root cell elongation by upregulating PECTIN METHYLESTERASE INHIBITOR 8 in Arabidopsis thaliana.PloS one · 2023Article
- Design of a Protein with Improved Thermal Stability by an Evolution-Based Generative Model.Angewandte Chemie (International ed. in English) · 2022Article
- Biochemical characterization of Pectin Methylesterase Inhibitor 3 fromCell surface (Amsterdam, Netherlands) · 2022Article
- Dynamics of cell wall polysaccharides during the elongation growth of rye primary roots.Planta · 2022Article
- Back From the Dead: The Atypical Kinase Activity of a Pseudokinase Regulator of Cation Fluxes During Inducible Immunity.Frontiers in plant science · 2022Article
- Overexpression ofFrontiers in plant science · 2022Article
- The Plant Invertase/Pectin Methylesterase Inhibitor Superfamily.Frontiers in plant science · 2022Review
- The role of pectin phase separation in plant cell wall assembly and growth.Cell surface (Amsterdam, Netherlands) · 2021Review
- Pectin Dependent Cell Adhesion Restored by a Mutant Microtubule Organizing Membrane Protein.Plants (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The fine-tuning of the degree of methylesterification of cell wall pectin is a key to regulating cell elongation and ultimately the shape of the plant body. Pectin methylesterification is spatiotemporally controlled by pectin methylesterases (PMEs; 66 members in Arabidopsis [Arabidopsis thaliana]). The comparably large number of proteinaceous pectin methylesterase inhibitors (PMEIs; 76 members in Arabidopsis) questions the specificity of the PME-PMEI interaction and the functional role of such abundance. To understand the difference, or redundancy, between PMEIs, we used molecular dynamics (MD) simulations to predict the behavior of two PMEIs that are coexpressed and have distinct effects on plant development: AtPMEI4 and AtPMEI9. Simulations revealed the structural determinants of the pH dependence for the interaction of these inhibitors with AtPME3, a major PME expressed in roots. Key residues that are likely to play a role in the pH dependence were identified. The predictions obtained from MD simulations were confirmed in vitro, showing that AtPMEI9 is a stronger, less pH-independent inhibitor compared with AtPMEI4. Using pollen tubes as a developmental model, we showed that these biochemical differences have a biological significance. Application of purified proteins at pH ranges in which PMEI inhibition differed between AtPMEI4 and AtPMEI9 had distinct consequences on pollen tube elongation. Therefore, MD simulations have proven to be a powerful tool to predict functional diversity between PMEIs, allowing the discovery of a strategy that may be used by PMEIs to inhibit PMEs in different microenvironmental conditions and paving the way to identify the specific role of PMEI diversity in muro.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.