ArticlePlant physiology2009
Characterization of the entire cystatin gene family in barley and their target cathepsin L-like cysteine-proteases, partners in the hordein mobilization during seed germination.
Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 168 citations in OpenAlex.
- Article
- Activity-Based Profiling of Papain-like Cysteine Proteases in Different Plant Organs During Barley Development.Plants (Basel, Switzerland) · 2026Article
- TMT Proteomics-Based Study of Proteins and Pathways Associated with β-Glucan Degradation in Barley Germination.Metabolites · 2026Article
- Expression profile of cystatin gene family in alfalfa (Medicago sativa L.) related to biotic and abiotic stress response.BMC genomics · 2025Article
- PhyCysID: Plant Cystatin Protein Prediction by an Artificial Intelligence Approach.Journal of chemical information and modeling · 2025Article
- Papain-like cysteine proteases inFrontiers in plant science · 2025Article
- Plant cathepsin B, a versatile protease.Frontiers in plant science · 2024Review
- MG1 interacts with a protease inhibitor and confers resistance to rice root-knot nematode.Nature communications · 2023Article
- Characterization and Differentiation of Grain Proteomes from Wild-Type Puroindoline and Variants in Wheat.Plants (Basel, Switzerland) · 2023Article
- Maquiberry Cystatins: Recombinant Expression, Characterization, and Use to Protect Tooth Dentin and Enamel.Biomedicines · 2023Article
- Synergistic Modulation of Seed Metabolites and Enzymatic Antioxidants Tweaks Moisture Stress Tolerance in Non-Cultivated Traditional Rice Genotypes during Germination.Plants (Basel, Switzerland) · 2022Article
- How Cysteine Protease GeneInternational journal of molecular sciences · 2021Article
- Genome-Wide Identification and Characterization of theInternational journal of molecular sciences · 2021Article
- Papain-like cysteine proteases are required for the regulation of photosynthetic gene expression and acclimation to high light stress.Journal of experimental botany · 2021Article
- Transcriptional control of local auxin distribution by the CsDFB1-CsPHB module regulates floral organogenesis in cucumber.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Citrus Vascular Proteomics Highlights the Role of Peroxidases and Serine Proteases during Huanglongbing Disease Progression.Molecular & cellular proteomics : MCP · 2020Article
- Genome-wide survey of soybean papain-like cysteine proteases and their expression analysis in root nodule symbiosis.BMC plant biology · 2020Article
- Review
- Article
8 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant cystatins are inhibitors of cysteine-proteases of the papain C1A and legumain C13 families. Cystatin data from multiple plant species have suggested that these inhibitors act as defense proteins against pests and pathogens and as regulators of protein turnover. In this study, we characterize the entire cystatin gene family from barley (Hordeum vulgare), which contain 13 nonredundant genes, and identify and characterize their target enzymes, the barley cathepsin L-like proteases. Cystatins and proteases were expressed and purified from Escherichia coli cultures. Each cystatin was found to have different inhibitory capability against barley cysteine-proteases in in vitro inhibitory assays using specific substrates. Real-time reverse transcription-polymerase chain reaction revealed that inhibitors and enzymes present a wide variation in their messenger RNA expression patterns. Their transcripts were mainly detected in developing and germinating seeds, and some of them were also expressed in leaves and roots. Subcellular localization of cystatins and cathepsin L-like proteases fused to green fluorescent protein demonstrated the presence of both protein families throughout the endoplasmic reticulum and the Golgi complex. Proteases and cystatins not only colocalized but also interacted in vivo in the plant cell, as revealed by bimolecular fluorescence complementation. The functional relationship between cystatins and cathepsin L-like proteases was inferred from their common implication as counterparts of mobilization of storage proteins upon barley seed germination. The opposite pattern of transcription expression in gibberellin-treated aleurones presented by inhibitors and enzymes allowed proteases to specifically degrade B, C, and D hordeins stored in the endosperm of barley seeds.
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