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The Binding Protein Associates with Monomeric Phaseolin.

A. Vitale1, A. Bielli, A. Ceriotti

  • 1Istituto Biosintesi Vegetali, Consiglio Nazionale delle Ricerche, via Bassini 15, 20133 Milano, Italy.

Plant Physiology
|April 1, 1995
PubMed
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Binding protein (BiP) associates with many plant secretory proteins during synthesis in the endoplasmic reticulum (ER). For phaseolin, BiP binds only monomers, indicating structural changes conceal binding sites during trimer formation.

Area of Science:

  • Plant Molecular Biology
  • Endoplasmic Reticulum Protein Folding
  • Secretory Pathway Dynamics

Background:

  • The endoplasmic reticulum (ER) is crucial for synthesizing and folding secretory proteins.
  • Binding protein (BiP) is a key chaperone involved in protein folding and quality control within the ER.
  • Understanding BiP's role is vital for deciphering plant protein maturation and transport.

Purpose of the Study:

  • To investigate the association of BiP with newly synthesized proteins in developing bean cotyledonary cells.
  • To explore the relationship between subunit assembly and BiP binding, specifically for the vacuolar glycoprotein phaseolin.
  • To elucidate the general role of BiP in plant secretory protein synthesis and maturation.

Main Methods:

  • Investigated ATP-sensitive association of BiP with various newly synthesized polypeptides in bean ER.

Related Experiment Videos

  • Analyzed the interaction of BiP with monomeric and trimeric forms of phaseolin.
  • Assessed the impact of BiP binding and trimerization on phaseolin transport.

    • Main Results:

    • Detected ATP-sensitive association of BiP with numerous newly synthesized polypeptides.
    • Observed that the extent of BiP association varies significantly among different proteins.
    • Found that only monomeric phaseolin, not trimers, associates with BiP, despite trimers being present in the ER.

    Conclusions:

    • BiP plays a general role in the synthesis of plant secretory proteins.
    • For phaseolin, BiP binding sites are masked during structural maturation (trimerization) in the ER.
    • Trimerization of phaseolin is not a rate-limiting step for its transport to storage vacuoles.