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Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor
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How do thermophilic proteins resist aggregation?

Anthony Mary Thangakani1, Sandeep Kumar, Devadasan Velmurugan

  • 1Department of Crystallography and Biophysics, University of Madras, Chennai, Tamil Nadu 600025, India.

Proteins
|March 6, 2012
PubMed
Summary

Thermophilic proteins, like their mesophilic counterparts, possess aggregation-prone regions (APRs). However, thermophilic proteins more effectively shield these APRs, enhancing protein stability and resistance to aggregation.

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Area of Science:

  • Protein biochemistry
  • Biophysics
  • Structural biology

Background:

  • Protein aggregation poses a significant threat to cellular function and viability across all life forms.
  • Maintaining native protein states is crucial for metabolic flux and cellular machinery operation.
  • Understanding aggregation resistance is key to protein stability and therapeutic applications.

Purpose of the Study:

  • To compare aggregation-resistance strategies in thermophilic proteins versus their mesophilic homologs.
  • To investigate the evolutionary mechanisms underlying protein aggregation avoidance.
  • To identify features contributing to enhanced protein stability at high temperatures.

Main Methods:

  • Comparative analysis of 373 protein families, including thermophilic and mesophilic homologs.
  • Bioinformatic identification of aggregation-prone regions (APRs) and amyloid-like fibril forming sequences.
  • Sequence and structural feature analysis to assess APR shielding strategies.

Main Results:

  • Both thermophilic and mesophilic proteins contain APRs, including amyloid-like fibril forming patterns.
  • Thermophilic proteins exhibit superior utilization of aggregation resistance strategies.
  • Thermophilic proteins more effectively sequester APRs within hydrophobic cores and utilize charged residues and proline for gatekeeping.
  • APRs are evolutionarily selected against and are not conserved between homologous thermophilic and mesophilic proteins.

Conclusions:

  • Thermophilic proteins possess enhanced intrinsic mechanisms for resisting aggregation compared to mesophilic proteins.
  • Evolution actively selects against amyloidogenic regions in proteins.
  • Findings have implications for the design of stable therapeutic proteins and antibodies.