Related Experiment Video
Updated: Aug 7, 2026
15:06
Synthesis of an Intein-mediated Artificial Protein Hydrogel
Published on: January 27, 2014
Were protein internal repeats formed by "bricolage"?
G Lavorgna1, L Patthy, E Boncinelli
1DIBIT, Istituto Scientifico H. S. Raffaele, Via Olgettina 60, 20132 Milan, Italy. giovanni.lavorgna@hsr.it
Trends in Genetics : TIG
|February 28, 2001
Summary
Evolution acts as a tinkerer, not an engineer. Genome analysis reveals that increased protein module repetition correlates with greater organismal complexity, suggesting adaptation of existing materials.
Area of Science:
- Evolutionary biology
- Genomics
- Molecular biology
Background:
- Evolutionary processes can be conceptualized as either "engineering" (designing anew) or "tinkering" (adapting existing components).
- Understanding the molecular basis of evolutionary complexity is a key challenge in biology.
Purpose of the Study:
- To investigate whether evolutionary processes favor adaptation of existing molecular "parts" or de novo design.
- To correlate genomic features with organismal complexity.
Main Methods:
- Analysis of completely sequenced genomes.
- Quantification of protein module repetition within genomes.
- Correlation analysis between protein module repetition and organismal complexity.
Main Results:
- Findings suggest evolution acts more like a "bricoleur" (tinkerer), utilizing and adapting existing molecular modules.
- A positive correlation was observed between the repetition of protein modules and the complexity of the organism.
- This indicates that increasing the number of existing functional units is a mechanism for evolving complexity.
Conclusions:
- Evolutionary complexity arises significantly from the adaptation and duplication of existing protein modules rather than entirely novel constructions.
- Genomic analysis supports the "tinkerer" model of evolution, highlighting the importance of modularity and repetition in protein evolution.
Related Concept Videos
01:22Protein Folding
Overview
01:22Protein Folding
Overview
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
01:25Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
00:55Fibrous Proteins
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...