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Intrinsic protein disorder in complete genomes.

A K Dunker1, Z Obradovic, P Romero

  • 1School of Molecular Biosciences, Washington State University, Pullman, WA 99164-4660, USA. dunker@disorder.chem.wsu.edu

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Summary

Eukaryotes exhibit higher percentages of intrinsically disordered protein segments compared to bacteria and archaea. This widespread protein disorder, particularly in eukaryotes, suggests a significant role in biological functions across diverse life forms.

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Area of Science:

  • Biochemistry
  • Genomics
  • Structural Biology

Background:

  • Intrinsic protein disorder describes protein regions or entire proteins that lack a stable three-dimensional structure.
  • Understanding the prevalence of protein disorder is crucial for comprehending protein function and evolution.

Purpose of the Study:

  • To predict and quantify intrinsically disordered protein segments and whole proteins across diverse genomes.
  • To compare the prevalence of protein disorder in bacteria, archaea, and eukaryotes.

Main Methods:

  • Computational prediction of disordered protein segments and wholly disordered proteins.
  • Analysis of protein sequences from 34 genomes (22 bacteria, 7 archaea, 5 eukaryotes).
  • Categorization of disordered regions by length thresholds (>= 50, >= 40, >= 30 amino acids).

Main Results:

  • Eukaryotes showed the highest percentages of disordered segments >= 50 amino acids (25-41%).
  • Wholly disordered proteins were estimated at 1-8% in bacteria and 2-11% (average 7%) in archaea.
  • Eukaryotes had estimates of wholly disordered proteins ranging from 3-17%.
  • Disordered proteins included ribosomal proteins and those with known or unknown functions.

Conclusions:

  • Intrinsic protein disorder is a common feature across bacteria, archaea, and eukaryotes.
  • Eukaryotes appear to possess a higher proportion of native protein disorder compared to prokaryotes.
  • Disordered proteins play diverse roles, including structural and functional capacities, across all domains of life.