Frequent transitions in self-assembly across the evolution of a central metabolic enzyme

Franziska L. Sendker, Tabea Schlotthauer, Christopher-Nils Mais, Yat Kei Lo, Mathias Girbig, Stefan Bohn, Thomas Heimerl, Daniel Schindler, Arielle Weinstein, Brian P. H. Metzger, Joseph W. Thornton, Arvind Pillai, Gert Bange, Jan M. Schuller and Georg K. A. Hochberg ()
Additional contact information
Franziska L. Sendker: Max-Planck-Institute for Terrestrial Microbiology
Tabea Schlotthauer: Max-Planck-Institute for Terrestrial Microbiology
Christopher-Nils Mais: Philipps-University Marburg
Yat Kei Lo: Philipps-University Marburg
Mathias Girbig: Max-Planck-Institute for Terrestrial Microbiology
Stefan Bohn: Helmholtz Munich
Thomas Heimerl: Philipps-University Marburg
Daniel Schindler: Philipps-University Marburg
Arielle Weinstein: University of Chicago
Brian P. H. Metzger: University of Chicago
Joseph W. Thornton: University of Chicago
Arvind Pillai: University of Chicago
Gert Bange: Max-Planck-Institute for Terrestrial Microbiology
Jan M. Schuller: Philipps-University Marburg
Georg K. A. Hochberg: Max-Planck-Institute for Terrestrial Microbiology

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract Many enzymes assemble into homomeric protein complexes comprising multiple copies of one protein. Because structural form is usually assumed to follow function in biochemistry, these assemblies are thought to evolve because they provide some functional advantage. In many cases, however, no specific advantage is known and, in some cases, quaternary structure varies among orthologs. This has led to the proposition that self-assembly may instead vary neutrally within protein families. The extent of such variation has been difficult to ascertain because quaternary structure has until recently been difficult to measure on large scales. Here, we employ mass photometry, phylogenetics, and structural biology to interrogate the evolution of homo-oligomeric assembly across the entire phylogeny of prokaryotic citrate synthases – an enzyme with a highly conserved function. We discover a menagerie of different assembly types that come and go over the course of evolution, including cases of parallel evolution and reversions from complex to simple assemblies. Functional experiments in vitro and in vivo indicate that evolutionary transitions between different assemblies do not strongly influence enzyme catalysis. Our work suggests that enzymes can wander relatively freely through a large space of possible assembly states and demonstrates the power of characterizing structure-function relationships across entire phylogenies.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-54408-6 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-54408-6

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-54408-6

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().