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Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy
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Adaptive evolution of signaling partners.

Daisuke Urano1, Taoran Dong2, Jeffrey L Bennetzen2

  • 1Department of Biology, University of North Carolina, Chapel Hill.

Molecular Biology and Evolution
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PubMed
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Protein interactions coevolve. A destabilizing mutation in one protein can be compensated by its partner, demonstrating evolutionary adaptation. This study reveals how one protein evolved to accommodate a mutation in its partner, maintaining function.

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coevolutionmolecular adaptationsignal transduction

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Area of Science:

  • Evolutionary biology
  • Molecular biology
  • Biochemistry

Background:

  • Protein interactions are crucial for biological functions and coevolve to maintain stability.
  • Mutations disrupting protein interactions can lead to counterselection unless compensated.
  • Heterotrimeric G protein signaling is a complex system involving protein interactions and conformational changes.

Purpose of the Study:

  • To investigate the coevolutionary path of interacting proteins following a destabilizing mutation.
  • To understand how compensatory mutations restore protein interaction and function.
  • To explore the evolutionary adaptation of Regulators of G protein Signaling (RGS) proteins in grasses.

Main Methods:

  • Comparative analysis of Gα subunits and RGS proteins across different plant species.
  • Biochemical assays to measure GTP hydrolysis rates and protein-protein interactions.
  • Structural analysis of protein interfaces to understand binding mechanisms.

Main Results:

  • Grasses possess Gα subunits with a destabilizing asparagine residue, unlike other plants.
  • The Setaria italica RGS protein (SiRGS1) can interact with both stabilizing and destabilizing Gα subunits.
  • SiRGS1 has adapted to the destabilizing Gα mutation by altering its binding pocket and not relying on the hydroxyl-bearing residue.

Conclusions:

  • Compensatory mutations in interacting proteins must tolerate both ancestral and derived structures.
  • SiRGS1 evolved to accommodate a deleterious mutation in grass Gα subunits, showcasing functional adaptation.
  • This study provides insights into the evolutionary constraints and adaptive strategies in protein interaction networks.