ArticleThe Journal of biological chemistry2012
Role of cysteine residues and disulfide bonds in the activity of a legume root nodule-specific, cysteine-rich peptide.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 95 citations in OpenAlex.
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- Exploring the role of symbiotic modifier peptidases in the legume - rhizobium symbiosis.Archives of microbiology · 2024Review
- Novel antimicrobial peptides identified in legume plant,Microbiology spectrum · 2024Article
- Evolution of antimicrobial cysteine-rich peptides in plants.Plant cell reports · 2023Article
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- Redox Regulation in Diazotrophic Bacteria in Interaction with Plants.Antioxidants (Basel, Switzerland) · 2021Review
- Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula.Scientific reports · 2021Article
- Symbiotic NCR Peptide Fragments Affect the Viability, Morphology and Biofilm Formation ofInternational journal of molecular sciences · 2021Article
- Study on the Inhibitory Activity of a Synthetic Defensin Derived from Barley Endosperm against Common Food Spoilage Yeast.Molecules (Basel, Switzerland) · 2020Article
- Potent Chimeric Antimicrobial Derivatives of theFrontiers in microbiology · 2020Article
- Unexplored Arsenals of Legume Peptides With Potential for Their Applications in Medicine and Agriculture.Frontiers in microbiology · 2020Review
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
The root nodules of certain legumes including Medicago truncatula produce >300 different nodule-specific cysteine-rich (NCR) peptides. Medicago NCR antimicrobial peptides (AMPs) mediate the differentiation of the bacterium, Sinorhizobium meliloti into a nitrogen-fixing bacteroid within the legume root nodules. In vitro, NCR AMPs such as NCR247 induced bacteroid features and exhibited antimicrobial activity against S. meliloti. The bacterial BacA protein is critical to prevent S. meliloti from being hypersensitive toward NCR AMPs. NCR AMPs are cationic and have conserved cysteine residues, which form disulfide (S-S) bridges. However, the natural configuration of NCR AMP S-S bridges and the role of these in the activity of the peptide are unknown. In this study, we found that either cysteine replacements or S-S bond modifications influenced the activity of NCR247 against S. meliloti. Specifically, either substitution of cysteines for serines, changing the S-S bridges from cysteines 1-2, 3-4 to 1-3, 2-4 or oxidation of NCR247 lowered its activity against S. meliloti. We also determined that BacA specifically protected S. meliloti against oxidized NCR247. Due to the large number of different NCRs synthesized by legume root nodules and the importance of bacterial BacA proteins for prolonged host infections, these findings have important implications for analyzing the function of these novel peptides and the protective role of BacA in the bacterial response toward these peptides.
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