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Sendker, F.L.* ; Schlotthauer, T.* ; Mais, C.N.* ; Lo, Y.K.* ; Girbig, M.* ; Bohn, S. ; Heimerl, T.* ; Schindler, D.* ; Weinstein, A.* ; Metzger, B.P.H.* ; Thornton, J.W.* ; Pillai, A.* ; Bange, G.* ; Schuller, J.M.* ; Hochberg, G.K.A.*

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

Nat. Commun. 15:10515 (2024)
Publ. Version/Full Text DOI PMC
Open Access Gold
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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.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Ii Citrate Synthase; Phylogenetic Analysis; Quaternary Structure; Crystal-structure; Glyoxylate Cycle; Cryo-em; Gene; Algorithms; Oligomers; Muscle
Language english
Publication Year 2024
HGF-reported in Year 2024
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Journal Nature Communications
Quellenangaben Volume: 15, Issue: 1, Pages: , Article Number: 10515 Supplement: ,
Publisher Nature Publishing Group
Publishing Place London
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503000-001
Grants ERC
European Union
NIH
Max-Planck Society
EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council)
DOI 10.1038/s41467-024-54408-6
WOS ID 001369778000023
Scopus ID 85211349378
PubMed ID 39627196
Erfassungsdatum 2024-12-06
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