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β-Propeller blades as ancestral peptides in protein evolution
Klaus O Kopec1, Andrei N Lupas
1Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, Tübingen, Baden-Württemberg, Germany.
Plos One
|October 22, 2013
Summary
This study reveals that the ancestral protein blade likely gave rise to both beta-propeller and type II beta-prism folds. These protein structures evolved from a common, ancient peptide fragment, highlighting early protein evolution.
Area of Science:
- Protein structure evolution
- Bioinformatics
- Molecular biology
Background:
- Beta-propeller protein folds are common, versatile scaffolds in nature.
- These folds consist of circular blades around a central pore.
- Sequence similarities suggest beta-propellers evolved from an ancestral blade.
Purpose of the Study:
- To investigate if the ancestral blade fragment could have given rise to other protein folds.
- To explore the evolutionary origins of protein structures.
Main Methods:
- Sequence comparison analysis to identify potential homologous proteins.
- Novel method correlating sequence and structure similarity to assess homology.
- Comparative analysis of beta-propellers, IRE1-LD, type II beta-prisms, beta-pinwheels, and WW domains.
Main Results:
- Identified homologous relationships between beta-propellers and inositol-requiring enzyme 1 luminal domain (IRE1-LD) and type II beta-prisms.
- Determined analogous relationships for beta-pinwheels and WW domains.
- IRE1-LD likely originated from a PQQ motif beta-propeller via fold-changing mutations.
- Type II beta-prisms likely arose from amplification of a single blade, possibly PQQ type.
Conclusions:
- Beta-propellers and type II beta-prisms originated from independent amplification of a blade-sized fragment.
- This fragment represents a remnant of an ancient peptide world.
- Provides insights into the early evolution of protein folds from simple peptides.
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