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Two γ-zeins induce the unfolded protein response.

Lorenzo Brocca1, Melania Zuccaro1, Giovanna Frugis2

  • 1Istituto di Biologia e Biotecnologia Agraria, Consiglio Nazionale delle Ricerche, Milano 20133, Italy.

Plant Physiology
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Different maize storage proteins, 16-kDa γ-zein and 27-kDa γ-zein, differentially activate the unfolded protein response (UPR) in Arabidopsis plants. 16-kDa γ-zein strongly induces UPR genes, while 27-kDa γ-zein shows a weaker effect, highlighting protein-specific UPR modulation.

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Area of Science:

  • Plant Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Seed development involves massive storage protein synthesis, stressing the endoplasmic reticulum (ER) and activating the unfolded protein response (UPR).
  • The specific contribution of different storage proteins to UPR activation remains unclear.

Purpose of the Study:

  • To investigate how distinct storage proteins, specifically maize γ-zeins and bean PHASEOLIN, differentially modulate the plant UPR.
  • To understand the protein-specific effects on UPR branches and downstream gene expression.

Main Methods:

  • Transgenic Arabidopsis plants expressing maize 16-kDa γ-zein, 27-kDa γ-zein, or bean PHASEOLIN were analyzed.
  • Quantitative PCR and protein blot analyses were used to assess UPR activation and the expression of UPR-controlled genes (e.g., BIP, GRP94, ERDJ3A).
  • The activation of specific UPR branches (bZIP60, bZIP28) and autophagy was examined.

Main Results:

  • 16-kDa γ-zein significantly activated the INOSITOL REQUIRING ENZYME1/BASIC LEUCINE ZIPPER 60 (bZIP60) UPR branch, leading to increased expression of folding helper genes.
  • 27-kDa γ-zein showed a weaker induction of UPR genes, primarily affecting BIP3 and ERDJ3A transcription.
  • Soluble proteins like PHASEOLIN and a mutated 27-kDa γ-zein did not significantly induce UPR, indicating the importance of protein properties and localization.

Conclusions:

  • Maize 16-kDa γ-zein is a potent inducer of the plant UPR, while 27-kDa γ-zein has a subtler effect, suggesting protein-specific modulation of UPR.
  • The differential UPR induction by storage proteins may have influenced their evolutionary adaptation regarding tissue and subcellular localization.
  • Understanding these mechanisms provides insights into plant stress responses and protein evolution.