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Loopy proteins appear conserved in evolution.

Jinfeng Liu1, Hepan Tan, Burkhard Rost

  • 1Department of Pharmacology, Columbia University, New York, NY 10032, USA.

Journal of Molecular Biology
|September 7, 2002
PubMed
Summary
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Proteins lacking regular secondary structure (NORS) are prevalent in eukaryotes and involved in crucial functions. These "loopy proteins" exhibit unique characteristics and evolutionary conservation, suggesting novel structural roles.

Area of Science:

  • Structural Biology
  • Bioinformatics
  • Evolutionary Biology

Background:

  • Many proteins lack stable structures, exhibiting flexibility that enables diverse functions.
  • Natively unfolded proteins are hypothesized to gain structure upon binding.
  • The functional significance of intrinsically disordered regions remains an active area of research.

Purpose of the Study:

  • To investigate proteins with long regions of no regular secondary structure (NORS).
  • To compare the prevalence and characteristics of NORS proteins across different domains of life.
  • To explore the functional and evolutionary implications of NORS regions.

Main Methods:

  • Bioinformatic analysis of protein sequences from 31 organisms.
  • Prediction and characterization of NORS regions (>70 residues).

Related Experiment Videos

  • Comparative analysis of amino acid composition, evolutionary conservation, and protein-protein interaction networks.
  • Main Results:

    • Proteins with NORS regions (loopy proteins) are significantly more abundant in eukaryotes (20%) than prokaryotes/archaea (4%).
    • NORS regions are often extensive (>150 residues) and possess distinct amino acid compositions compared to known protein loops.
    • NORS proteins show higher evolutionary conservation and increased protein-protein interactions, particularly in yeast.
    • Regulatory and transcription-related functions are enriched in loopy proteins, while biosynthesis and energy metabolism are under-represented.

    Conclusions:

    • NORS proteins are functionally significant and prevalent, especially in eukaryotes.
    • These proteins may adopt novel structural conformations beyond current understanding.
    • The study highlights the importance of intrinsically disordered regions in protein function and evolution.