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Dehydrin Client Proteins Identified Using Phage Display Affinity Selected Libraries Processed With Paired-End Phage

Sandra Helena Unêda-Trevisoli1, Lynnette M A Dirk2, Francisco Elder Carlos Bezerra Pereira3

  • 1Department of Horticulture, Martin-Gatton College of Agriculture, Food and Environment, University of Kentucky, Lexington, Kentucky, USA; Seed Biology Program, University of Kentucky, Lexington, Kentucky, USA; Department of Crop Production, São Paulo State University (Unesp), School of Agricultural and Veterinarian Sciences, São Paulo, Brazil.

Molecular & Cellular Proteomics : MCP
|October 23, 2024
PubMed
Summary
This summary is machine-generated.

Late embryogenesis abundant proteins (LEAPs) bind to specific client proteins (CtPs), revealing their protective mechanisms. This study identified common LEAP targets in plants, offering insights into abiotic stress tolerance.

Keywords:
client proteinslate embryogenesis abundant proteinspaired-end sequencingphage displaytemperature related intensity change assay

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Area of Science:

  • Plant molecular biology
  • Protein biochemistry
  • Abiotic stress response

Background:

  • Late embryogenesis abundant proteins (LEAPs) are intrinsically disordered proteins implicated in abiotic stress tolerance.
  • LEAP function is thought to involve binding to client proteins (CtPs) for protection, but specific CtPs remain largely unidentified.
  • Understanding LEAP-CtP interactions is crucial for elucidating their protective mechanisms.

Purpose of the Study:

  • To identify client proteins (CtPs) that bind to LEAP orthologs from Arabidopsis and soybean.
  • To characterize the binding domains of CtPs interacting with LEAPs.
  • To validate LEAP-CtP interactions using independent experimental methods.

Main Methods:

  • Phage display affinity selection was employed to screen plant protein libraries against LEAP orthologs.
  • High-throughput sequencing of affinity-purified phage was used to identify LEAP-binding proteins.
  • In planta bimolecular fluorescence complementation (BiFC) assays and temperature-related intensity change analysis were used for validation.

Main Results:

  • A common repertoire of LEAP-binding CtPs was identified between Arabidopsis and soybean LEAP orthologs.
  • The study revealed specific domains within CtPs, including dehydrin Y-segments and K-domains, involved in LEAP binding.
  • LEAP:CtP interactions were confirmed in planta, validating the phage display findings.

Conclusions:

  • The findings identify novel LEAP client proteins and elucidate the molecular basis of LEAP-CtP interactions.
  • This work provides critical insights into the role of LEAPs in protein protection and abiotic stress tolerance in plants.
  • The identified LEAP-CtP interactions offer potential targets for engineering enhanced stress resilience in crops.