ArticleThe Journal of biological chemistry2010
Arabidopsis AtSerpin1, crystal structure and in vivo interaction with its target protease RESPONSIVE TO DESICCATION-21 (RD21).
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 81 citations in OpenAlex.
- RD21-like proteases: key effector hubs in plant-pathogen interactions.Journal of experimental botany · 2025Review
- GbSER02 Interacts With GhVOZ1 to Promote Fiber Elongation by Modulating Gibberellin Synthesis in Cotton.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Targeting Magnaporthe oryzae effector MoErs1 and host papain-like protease OsRD21 interaction to combat rice blast.Nature plants · 2024Article
- TcSERPIN, an inhibitor that interacts with cocoa defense proteins and has biotechnological potential against human pathogens.Frontiers in plant science · 2024Article
- Plant Serpins: Potential Inhibitors of Serine and Cysteine Proteases with Multiple Functions.Plants (Basel, Switzerland) · 2023Review
- Genes Encoding Structurally Conserved Serpins in the Wheat Genome: Identification and Expression Profiles during Plant Development and Abiotic and Biotic Stress.International journal of molecular sciences · 2023Article
- Proteomic Analysis of Embryo Isolated From MatureFrontiers in plant science · 2022Article
- Spatial distribution of proteins and metabolites in developing wheat grain and their differential regulatory response during the grain filling process.The Plant journal : for cell and molecular biology · 2021Article
- A Comprehensive Phylogenetic Analysis of the Serpin Superfamily.Molecular biology and evolution · 2021Article
- EMS Derived Wheat Mutant BIG8-1 (International journal of molecular sciences · 2021Article
- Genome Wide Identification and Comparative Analysis of the Serpin Gene Family in Brachypodium and Barley.Plants (Basel, Switzerland) · 2020Article
- Peptide-based protease inhibitors from plants.Drug discovery today · 2019Review
- A fungal substrate mimicking molecule suppresses plant immunity via an inter-kingdom conserved motif.Nature communications · 2019Article
- Chloroplast Protein Degradation in Senescing Leaves: Proteases and Lytic Compartments.Frontiers in plant science · 2019Review
- Singlet Oxygen Plays an Essential Role in the Root's Response to Osmotic Stress.Plant physiology · 2018Article
- Noncanonical interactions between serpin and β-amylase in barley grain improve β-amylase activityPlant direct · 2018Article
- Article
- The complex world of plant protease inhibitors: Insights into a Kunitz-type cysteine protease inhibitor ofCommunicative & integrative biology · 2018Review
- Serpin1 and WSCP differentially regulate the activity of the cysteine protease RD21 during plant development inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Major Cys protease activities are not essential for senescence in individually darkened Arabidopsis leaves.BMC plant biology · 2017Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
In animals, protease inhibitors of the serpin family are associated with many physiological processes, including blood coagulation and innate immunity. Serpins feature a reactive center loop (RCL), which displays a protease target sequence as a bait. RCL cleavage results in an irreversible, covalent serpin-protease complex. AtSerpin1 is an Arabidopsis protease inhibitor that is expressed ubiquitously throughout the plant. The x-ray crystal structure of recombinant AtSerpin1 in its native stressed conformation was determined at 2.2 A. The electrostatic surface potential below the RCL was found to be highly positive, whereas the breach region critical for RCL insertion is an unusually open structure. AtSerpin1 accumulates in plants as a full-length and a cleaved form. Fractionation of seedling extracts by nonreducing SDS-PAGE revealed the presence of an additional slower migrating complex that was absent when leaves were treated with the specific cysteine protease inhibitor L-trans-epoxysuccinyl-L-leucylamido (4-guanidino)butane. Significantly, RESPONSIVE TO DESICCATION-21 (RD21) was the major protease labeled with the L-trans-epoxysuccinyl-L-leucylamido (4-guanidino)butane derivative DCG-04 in wild type extracts but not in extracts of mutant plants constitutively overexpressing AtSerpin1, indicating competition. Fractionation by nonreducing SDS-PAGE followed by immunoblotting with RD21-specific antibody revealed that the protease accumulated both as a free enzyme and in a complex with AtSerpin1. Importantly, both RD21 and AtSerpin1 knock-out mutants lacked the serpin-protease complex. The results establish that the major Arabidopsis plant serpin interacts with RD21. This is the first report of the structure and in vivo interaction of a plant serpin with its target protease.
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