ArticleProtein science : a publication of the Protein Society2008
The structure of "defective in induced resistance" protein of Arabidopsis thaliana, DIR1, reveals a new type of lipid transfer protein.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed, 93 citations in OpenAlex.
- Plant Non-Specific Lipid Transfer Proteins (nsLTPs): Comprehensive Functional Analysis and Defense Mechanisms.Biology · 2026Review
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- The Dynamic Changes in Biosynthesis and Spatiotemporal Distribution of Phytohormones Under Jasmonic Acid Treatment Provide Insights into Hormonal Regulation inPlants (Basel, Switzerland) · 2025Article
- Roles of non-specific lipid transfer proteins in plant defense: structural and functional perspectives.Frontiers in fungal biology · 2025Review
- Genome-Wide Identification of Common BeanGenes · 2022Article
- Lipid transfer proteins involved in plant-pathogen interactions and their molecular mechanisms.Molecular plant pathology · 2022Review
- A successful defense of the narrow-leafed lupin against anthracnose involves quick and orchestrated reprogramming of oxidation-reduction, photosynthesis and pathogenesis-related genes.Scientific reports · 2022Article
- WIPK-NtLTP4 pathway confers resistance to Ralstonia solanacearum in tobacco.Plant cell reports · 2022Article
- Lipid Transfer Proteins (LTPs)-Structure, Diversity and Roles beyond Antimicrobial Activity.Antibiotics (Basel, Switzerland) · 2021Review
- Genome-wide identification and expression profile under abiotic stress of the barley non-specific lipid transfer protein gene family and its Qingke Orthologues.BMC genomics · 2021Article
- Signals in systemic acquired resistance of plants against microbial pathogens.Molecular biology reports · 2021Review
- The Resistance of Narrow-Leafed Lupin toInternational journal of molecular sciences · 2021Article
- Identification of DIR1-Dependant Cellular Responses in Guard Cell Systemic Acquired Resistance.Frontiers in molecular biosciences · 2021Article
- Multi-Omics Revealed Molecular Mechanisms Underlying Guard Cell Systemic Acquired Resistance.International journal of molecular sciences · 2020Article
- Transcriptome Analysis of Choke Stroma and Asymptomatic Inflorescence Tissues Reveals Changes in Gene Expression in BothMicroorganisms · 2019Article
- Non-Specific Lipid Transfer Proteins inPathogens (Basel, Switzerland) · 2019Article
- Genome-wide identification, characterization and expression analysis of the non-specific lipid transfer proteins in potato.BMC genomics · 2019Article
- Plant immune responses - from guard cells and local responses to systemic defense against bacterial pathogens.Plant signaling & behavior · 2019Review
- Wheat TaMs1 is a glycosylphosphatidylinositol-anchored lipid transfer protein necessary for pollen development.BMC plant biology · 2018Article
- The major nectar protein of Brassica rapa is a non-specific lipid transfer protein, BrLTP2.1, with strong antifungal activity.Journal of experimental botany · 2018Article
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Screening of transfer DNA (tDNA) tagged lines of Arabidopsis thaliana for mutants defective in systemic acquired resistance led to the characterization of dir1-1 (defective in induced resistance [systemic acquired resistance, SAR]) mutant. It has been suggested that the protein encoded by the dir1 gene, i.e., DIR1, is involved in the long distance signaling associated with SAR. DIR1 displays the cysteine signature of lipid transfer proteins, suggesting that the systemic signal could be lipid molecules. However, previous studies have shown that this signature is not sufficient to define a lipid transfer protein, i.e., a protein capable of binding lipids. In this context, the lipid binding properties and the structure of a DIR1-lipid complex were both determined by fluorescence and X-ray diffraction. DIR1 is able to bind with high affinity two monoacylated phospholipids (dissociation constant in the nanomolar range), mainly lysophosphatidyl cholines, side-by-side in a large internal tunnel. Although DIR1 shares some structural and lipid binding properties with plant LTP2, it displays some specific features that define DIR1 as a new type of plant lipid transfer protein. The signaling function associated with DIR1 may be related to a specific lipid transport that needs to be characterized and to an additional mechanism of recognition by a putative receptor, as the structure displays on the surface the characteristic PxxP structural motif reminiscent of SH3 domain signaling pathways.
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