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

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 pr

SUBMITTER: Sendker FL 

PROVIDER: S-EPMC11245102 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature