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Protein tandem repeats - the more perfect, the less structured
Julien Jorda1, Bin Xue, Vladimir N Uversky
1Centre de Recherches de Biochimie Macromoléculaire, CNRS UMR-5237, University of Montpellier 1 and 2, France.
The FEBS Journal
|June 18, 2010
Summary
Perfect tandem repeats are rare in natural proteins, suggesting they are recent evolutionary events. Imperfect repeats are more common and tend to be less structured.
Area of Science:
- Structural biology
- Bioinformatics
- Evolutionary biology
Background:
- Tandem repeats are common in proteins but their structural properties are not fully understood.
- Perfect tandem repeats are rarely observed in naturally occurring proteins with known 3D structures.
Purpose of the Study:
- To analyze the structural properties of protein regions with perfect and nearly perfect tandem repeats.
- To investigate the correlation between repeat perfection and protein structure/disorder.
- To explore the evolutionary implications of tandem repeat perfection.
Main Methods:
- Analysis of protein structures in the Protein Data Bank (PDB).
- Prediction of intrinsic disorder in tandem repeats using SwissProt protein data.
- Comparative analysis across species and subcellular localizations.
Main Results:
- Perfect tandem repeats are predominantly found in de novo designed proteins, not natural ones.
- Natural protein structure abundance is inversely correlated with repeat perfection.
- Higher repeat perfection correlates with a greater tendency for intrinsic disorder.
- Tandem repeat disorder varies across species and subcellular locations, with distinct patterns in prokaryotes and eukaryotes.
Conclusions:
- Repeat perfection in tandem repeats is likely indicative of recent evolutionary events.
- Perfection does not necessarily imply exceptional structural or functional importance.
- The structural state of tandem repeats is influenced by evolutionary history and cellular context.
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