Emergence of fractal geometries in the evolution of a metabolic enzyme.
Nature
; 628(8009): 894-900, 2024 Apr.
Article
de En
| MEDLINE
| ID: mdl-38600380
ABSTRACT
Fractals are patterns that are self-similar across multiple length-scales1. Macroscopic fractals are common in nature2-4; however, so far, molecular assembly into fractals is restricted to synthetic systems5-12. Here we report the discovery of a natural protein, citrate synthase from the cyanobacterium Synechococcus elongatus, which self-assembles into Sierpinski triangles. Using cryo-electron microscopy, we reveal how the fractal assembles from a hexameric building block. Although different stimuli modulate the formation of fractal complexes and these complexes can regulate the enzymatic activity of citrate synthase in vitro, the fractal may not serve a physiological function in vivo. We use ancestral sequence reconstruction to retrace how the citrate synthase fractal evolved from non-fractal precursors, and the results suggest it may have emerged as a harmless evolutionary accident. Our findings expand the space of possible protein complexes and demonstrate that intricate and regulatable assemblies can evolve in a single substitution.
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Citrate (si)-synthase
/
Fractales
/
Évolution moléculaire
/
Synechococcus
/
Multimérisation de protéines
Langue:
En
Journal:
Nature
Année:
2024
Type de document:
Article
Pays d'affiliation:
Allemagne
Pays de publication:
Royaume-Uni