Emergence of fractal geometries in the evolution of a metabolic enzyme

Sendker, Franziska L. and Lo, Yat Kei and Heimerl, Thomas and Bohn, Stefan and Persson, Louise J. and Mais, Christopher-Nils and Sadowska, Wiktoria and Paczia, Nicole and Nußbaum, Eva and del Carmen Sánchez Olmos, María and Forchhammer, Karl and Schindler, Daniel and Erb, Tobias J. and Benesch, Justin L. P. and Marklund, Erik G. and Bange, Gert and Schuller, Jan M. and Hochberg, Georg K. A. (2024) Emergence of fractal geometries in the evolution of a metabolic enzyme. Nature. ISSN 0028-0836

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Abstract

Fractals are patterns that are self-similar across multiple length-scales1. Macroscopic fractals are common in nature2,3,4; however, so far, molecular assembly into fractals is restricted to synthetic systems5,6,7,8,9,10,11,12. Here we report the discovery of a natural protein, citrate synthase from the cyanobacterium Synechococcus elongatus, which self-assembles into Sierpiński 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.

Item Type: Article
Subjects: EP Archives > Multidisciplinary
Depositing User: Managing Editor
Date Deposited: 11 Apr 2024 09:04
Last Modified: 11 Apr 2024 09:04
URI: http://research.send4journal.com/id/eprint/3853

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