ArticlePlant physiology2013
The nodulation factor hydrolase of Medicago truncatula: characterization of an enzyme specifically cleaving rhizobial nodulation signals.
Article in Plant physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- Exploring symbiotic legume-rhizobia relationships across tropical species.World journal of microbiology & biotechnology · 2026Article
- Chitinase-activity-independent anti-insect effect of class V chitinase from fig trees (Ficus carica).Planta · 2025Article
- Genome-Wide Identification and Expression Analyses ofInternational journal of molecular sciences · 2025Article
- A soybean cyst nematode suppresses microbial plant symbionts using a lipochitooligosaccharide-hydrolysing enzyme.Nature microbiology · 2024Article
- CRISPR/Cas9-Mediated Generation of Mutant Lines inBiology · 2024Article
- Laser Capture Microdissection Transcriptome Reveals Spatiotemporal Tissue Gene Expression Patterns ofMolecular plant-microbe interactions : MPMI · 2023Article
- Oxidative Status ofInternational journal of molecular sciences · 2023Article
- Legumes Regulate Symbiosis with Rhizobia via Their Innate Immune System.International journal of molecular sciences · 2023Review
- Editorial: Metabolic adjustments and gene expression reprogramming for symbiotic nitrogen fixation in legume nodules, volume II.Frontiers in plant science · 2023Article
- Nod factor perception: an integrative view of molecular communication during legume symbiosis.Plant molecular biology · 2022Review
- TheFrontiers in plant science · 2022Article
- Goldilocks Principle: MtNFH1 Ensures Optimal Nod Factor Activity.The Plant cell · 2018Article
- Role of the Nod Factor Hydrolase MtNFH1 in Regulating Nod Factor Levels during Rhizobial Infection and in Mature Nodules ofThe Plant cell · 2018Article
- A Laser Dissection-RNAseq Analysis Highlights the Activation of Cytokinin Pathways by Nod Factors in the Medicago truncatula Root Epidermis.Plant physiology · 2016Article
- A single amino acid substitution in a chitinase of the legume Medicago truncatula is sufficient to gain Nod-factor hydrolase activity.Open biology · 2016Article
- The small GTPase ROP10 of Medicago truncatula is required for both tip growth of root hairs and nod factor-induced root hair deformation.The Plant cell · 2015Article
- The root hair "infectome" of Medicago truncatula uncovers changes in cell cycle genes and reveals a requirement for Auxin signaling in rhizobial infection.The Plant cell · 2014Article
- The role of the cell wall compartment in mutualistic symbioses of plants.Frontiers in plant science · 2014Review
- Genetic Insights Into Pathways Supporting Optimized Biological Nitrogen Fixation in Chickpea and Their Interaction With Disease Resistance Breeding.Physiologia plantarumArticle
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nodule formation induced by nitrogen-fixing rhizobia depends on bacterial nodulation factors (NFs), modified chitin oligosaccharides with a fatty acid moiety. Certain NFs can be cleaved and inactivated by plant chitinases. However, the most abundant NF of Sinorhizobium meliloti, an O-acetylated and sulfated tetramer, is resistant to hydrolysis by all plant chitinases tested so far. Nevertheless, this NF is rapidly degraded in the host rhizosphere. Here, we identify and characterize MtNFH1 (for Medicago truncatula Nod factor hydrolase 1), a legume enzyme structurally related to defense-related class V chitinases (glycoside hydrolase family 18). MtNFH1 lacks chitinase activity but efficiently hydrolyzes all tested NFs of S. meliloti. The enzyme shows a high cleavage preference, releasing exclusively lipodisaccharides from NFs. Substrate specificity and kinetic properties of MtNFH1 were compared with those of class V chitinases from Arabidopsis (Arabidopsis thaliana) and tobacco (Nicotiana tabacum), which cannot hydrolyze tetrameric NFs of S. meliloti. The Michaelis-Menten constants of MtNFH1 for NFs are in the micromolar concentration range, whereas nonmodified chitin oligosaccharides represent neither substrates nor inhibitors for MtNFH1. The three-dimensional structure of MtNFH1 was modeled on the basis of the known structure of class V chitinases. Docking simulation of NFs to MtNFH1 predicted a distinct binding cleft for the fatty acid moiety, which is absent in the class V chitinases. Point mutation analysis confirmed the modeled NF-MtNFH1 interaction. Silencing of MtNFH1 by RNA interference resulted in reduced NF degradation in the rhizosphere of M. truncatula. In conclusion, we have found a novel legume hydrolase that specifically inactivates NFs.
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