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Regulation, evolution and consequences of cotranslational protein complex assembly.

Eviatar Natan1, Jonathan N Wells2, Sarah A Teichmann3

  • 1Department of Chemistry, University of Oxford, 12 Mansfield Rd, Oxford OX1 3TA, UK.

Current Opinion in Structural Biology
|December 15, 2016
PubMed
Summary

Protein complexes assemble during translation to prevent cellular damage. This cotranslational assembly is regulated to ensure efficient protein complex formation and avoid harmful aggregation, with implications for genetic disorders.

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Protein complexes are essential for nearly all cellular functions.
  • Proper assembly is critical for cell viability.
  • Misfolded proteins can lead to aggregation and cellular dysfunction.

Purpose of the Study:

  • To review the process of cotranslational assembly of protein complexes.
  • To discuss the regulation of cotranslational assembly.
  • To explore the implications of cotranslational assembly for dominant-negative genetic disorders.

Main Methods:

  • Literature review of cotranslational assembly mechanisms.
  • Analysis of regulatory strategies for protein complex formation.
  • Discussion of the impact of cotranslational assembly on protein fate and disease.

Main Results:

  • Cotranslational assembly ensures efficient formation of protein complexes.
  • Regulatory mechanisms prevent non-specific interactions and aggregation.
  • Disruptions in cotranslational assembly can contribute to genetic disorders.

Conclusions:

  • Cotranslational assembly is a vital process for maintaining cellular health.
  • Understanding cotranslational assembly regulation is key to addressing protein misfolding diseases.
  • This process has significant implications for the inheritance of dominant-negative genetic disorders.