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Updated: Jun 2, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Conserved residues in the ankyrin domain of VAPYRIN indicate potential protein-protein interaction surfaces

Nadja Feddermann1, Didier Reinhardt

  • 1Department of Biology, University of Fribourg, Fribourg, Switzerland.

Plant Signaling & Behavior
|April 20, 2011
PubMed

Insights

Plant VAPYRIN proteins are crucial for establishing symbiotic relationships with beneficial microbes. Mutations in VAPYRIN disrupt the accommodation of arbuscular mycorrhiza fungi and rhizobia, hindering nutrient exchange and symbiosis.

Area of Science:

  • Plant biology
  • Microbial symbiosis
  • Molecular genetics

Background:

  • Plant VAPYRIN proteins are essential for establishing arbuscular mycorrhiza (AM) and root nodule symbiosis (RNS).
  • Vapyrin mutants exhibit impaired intracellular accommodation of AM fungi and rhizobia.
  • AM symbiosis is critical for plant nutrient uptake, with arbuscules serving as the primary site for nutrient exchange.

Purpose of the Study:

  • To investigate the role of VAPYRIN proteins in plant-microbe symbiosis.
  • To analyze the conserved structure of VAPYRIN proteins across different plant species.
  • To identify potential functional domains and binding sites within VAPYRIN proteins.

Main Methods:

  • Comparative analysis of VAPYRIN protein sequences from dicots, monocots, and Physcomitrella patens.
  • Structural analysis of the ankyrin domain of VAPYRIN proteins.
  • Identification of conserved residues and surface patches within the ankyrin domain.

Main Results:

  • VAPYRIN proteins possess a conserved domain structure comprising a major sperm protein (MSP) and ankyrin domains.
  • The ankyrin domain of plant VAPYRINS shows resemblance to the human ankyrin R D34 domain.
  • Conserved residues in the petunia VAPYRIN ankyrin domain cluster on a surface patch, suggesting a conserved binding site.

Conclusions:

  • The conserved ankyrin domain of VAPYRIN proteins likely plays a critical role in forming protein complexes.
  • This protein complex is essential for the intracellular accommodation of microbial endosymbionts in plant symbiotic associations.
  • VAPYRIN proteins represent a conserved mechanism for managing beneficial microbial interactions in plants.

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