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Folding cooperativity and allosteric function in the tandem-repeat protein class.

Albert Perez-Riba1, Marie Synakewicz1, Laura S Itzhaki2

  • 1Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, UK.

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|May 9, 2018
PubMed
Summary
This summary is machine-generated.

Allostery, or action at a distance, is key to understanding how tandem-repeat proteins like tetratricopeptide repeats (TPRs) fold cooperatively and function as allosteric switches. This mechanism regulates vital cellular processes, including bacterial quorum sensing.

Keywords:
Rap proteinsallosteryelastic network modelsmolecular switchesprotein cooperativityrepeat proteins

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Area of Science:

  • Biophysics
  • Structural Biology
  • Molecular Biology

Background:

  • Allostery describes structural changes distant from a binding site, extensively studied in enzymology.
  • Tandem-repeat proteins, such as tetratricopeptide repeats (TPRs) and ankyrin repeats, exhibit cooperative folding and allosteric regulation.
  • These proteins act as scaffolds, mediating allosteric effects through their repeat arrays to control multi-subunit enzyme activity.

Purpose of the Study:

  • To explore the concept of action at a distance in tandem-repeat protein folding and function.
  • To connect the folding cooperativity of these proteins with their mechanisms as allosteric switches.
  • To discuss common underlying principles governing these phenomena.

Main Methods:

  • Conceptual review and synthesis of existing research on allostery and tandem-repeat proteins.
  • Analysis of structural data for repeat-protein scaffolds.
  • Highlighting recent findings on RRPNN subclass of TPRs.

Main Results:

  • Tandem-repeat proteins demonstrate cooperative folding despite nearest-neighbor interactions.
  • Repeat arrays can transmit allosteric effects, influencing enzyme activity.
  • Specific TPR subclasses, like RRPNN, act as allosteric switches modulating bacterial quorum sensing.

Conclusions:

  • Folding cooperativity and allosteric switch mechanisms in tandem-repeat proteins are intrinsically linked.
  • Understanding these intertwined principles offers insights into molecular machines and allosteric regulation.
  • Allostery in repeat proteins has broad implications for cellular regulation and signaling pathways.