ArticlePlant physiology2006
Polygalacturonase-inhibiting protein interacts with pectin through a binding site formed by four clustered residues of arginine and lysine.
Article in Plant physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
39 citing papers in PubMed, 93 citations in OpenAlex.
- Article
- Signals and Their Perception for Remodelling, Adjustment and Repair of the Plant Cell Wall.International journal of molecular sciences · 2023Review
- STOP1 and STOP1-like proteins, key transcription factors to cope with acid soil syndrome.Frontiers in plant science · 2023Review
- Plant Cell Wall Integrity Perturbations and Priming for Defense.Plants (Basel, Switzerland) · 2022Review
- Exploring the potential of engineering polygalacturonase-inhibiting protein as an ecological, friendly, and nontoxic pest control agent.Biotechnology and bioengineering · 2021Article
- Expression GWAS ofFrontiers in plant science · 2021Article
- New Players in the Interaction Between Beetle Polygalacturonases and Plant Polygalacturonase-Inhibiting Proteins: Insights From Proteomics and Gene Expression Analyses.Frontiers in plant science · 2021Article
- Direct evidence for a new mode of plant defense against insects via a novel polygalacturonase-inhibiting protein expression strategy.The Journal of biological chemistry · 2020Article
- Article
- Digging for Stress-Responsive Cell Wall Proteins for Developing Stress-Resistant Maize.Frontiers in plant science · 2020Article
- Changes in the Proteome ofInternational journal of molecular sciences · 2018Article
- Damage-associated responses of the host contribute to defence against cyst nematodes but not root-knot nematodes.Journal of experimental botany · 2017Article
- Molecular evidence for the involvement of a polygalacturonase-inhibiting protein, GhPGIP1, in enhanced resistance to Verticillium and Fusarium wilts in cotton.Scientific reports · 2017Article
- Didehydrophenylalanine, an abundant modification in the beta subunit of plant polygalacturonases.PloS one · 2017Article
- Review
- Evaluation of the significance of cell wall polymers in flax infected with a pathogenic strain of Fusarium oxysporum.BMC plant biology · 2016Article
- Arabidopsis leucine-rich repeat extensin (LRX) proteins modify cell wall composition and influence plant growth.BMC plant biology · 2015Article
- An update on polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein that protects crop plants against pathogens.Frontiers in plant science · 2015Review
- A receptor-like protein mediates the response to pectin modification by activating brassinosteroid signaling.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Homogalacturonan-modifying enzymes: structure, expression, and roles in plants.Journal of experimental botany · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polygalacturonase-inhibiting protein (PGIP) is a cell wall protein that inhibits fungal polygalacturonases (PGs) and retards the invasion of plant tissues by phytopathogenic fungi. Here, we report the interaction of two PGIP isoforms from Phaseolus vulgaris (PvPGIP1 and PvPGIP2) with both polygalacturonic acid and cell wall fractions containing uronic acids. We identify in the three-dimensional structure of PvPGIP2 a motif of four clustered arginine and lysine residues (R183, R206, K230, and R252) responsible for this binding. The four residues were mutated and the protein variants were expressed in Pichia pastoris. The ability of both wild-type and mutated proteins to bind pectins was investigated by affinity chromatography. Single mutations impaired the binding and double mutations abolished the interaction, thus indicating that the four clustered residues form the pectin-binding site. Remarkably, the binding of PGIP to pectin is displaced in vitro by PGs, suggesting that PGIP interacts with pectin and PGs through overlapping although not identical regions. The specific interaction of PGIP with polygalacturonic acid may be strategic to protect pectins from the degrading activity of fungal PGs.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.