Recombinant Arabidopsis lyrata subsp. lyrata CASP-like protein ARALYDRAFT_477942 (ARALYDRAFT_477942)

Overview of Recombinant Arabidopsis lyrata subsp. lyrata CASP-like Protein ARALYDRAFT_477942

Recombinant Arabidopsis lyrata subsp. lyrata CASP-like protein ARALYDRAFT_477942 is a synthetically produced integral membrane protein belonging to the Casparian strip membrane domain (CASP) family . These proteins are critical for forming Casparian strips—lignin-based barriers in plant root endodermal cells that regulate nutrient absorption and stress responses . The recombinant variant is expressed using cell-free systems or heterologous hosts (e.g., E. coli, yeast) and purified to ≥85% purity .

Gene Information

• Gene name: ARALYDRAFT_477942

• Orthologs: Shares homology with At3g55390 (AtCASPL4C1) in Arabidopsis thaliana .

• Evolutionary context: Phylogenetically clusters within the CASP family subgroup associated with Casparian strip formation .

Protein Features

The protein contains four transmembrane helices (residues 45–67, 87–109, 130–149, 169–191), typical of CASP-family proteins .

Key Domains

• Extracellular Loop 1 (EL1): Contains a conserved nine-amino-acid signature (ESLPFFTQF) critical for endodermis-specific localization .

• Extracellular Loop 2 (EL2): Mutations in residues (e.g., W164G) disrupt membrane domain localization, highlighting functional importance .

Functional Role

• Casparian strip formation: Likely participates in scaffolding lignin polymerization machinery at endodermal plasma membranes, similar to AtCASP1-5 .

• Stress responses: CASP-like proteins in related species (e.g., watermelon ClCASPL) show cold-induced expression patterns, suggesting roles in abiotic stress adaptation .

Production Systems

• Hosts: Cell-free expression, E. coli, yeast, or mammalian cells .

• Purity: ≥85% (SDS-PAGE verified) .

• Storage: Tris-based buffer with 50% glycerol at -20°C or -80°C .

Sequence Information

The full-length construct (1–200 residues) includes the N-terminal sequence:
MASTENPDPETGKSEPIPASATTPPPSAASFLDCRKIDVIIRVLLFSATLTALIVMVTSD... .

Comparative Analysis with Orthologs

Data synthesized from .

Research Applications

1. Mechanistic studies: Used to dissect CASP-family protein interactions in membrane domain assembly .

2. Biotechnological engineering: Potential target for modifying nutrient uptake efficiency in crops .

3. Structural biology: Serves as a template for transmembrane protein crystallization trials .

Open Questions and Future Directions

• Functional validation: Direct evidence of ARALYDRAFT_477942’s role in Casparian strip formation is lacking .

• Regulatory networks: Interactions with lignin biosynthesis enzymes (e.g., peroxidases) remain unexplored .

• Stress adaptation: Links to drought or salinity tolerance require investigation .