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- Title
Structural and evolutionary versatility in protein complexes with uneven stoichiometry.
- Authors
Marsh, Joseph A.; Rees, Holly A.; Ahnert, Sebastian E.; Teichmann, Sarah A.
- Abstract
Proteins assemble into complexes with diverse quaternary structures. Although most heteromeric complexes of known structure have even stoichiometry, a significant minority have uneven stoichiometry—that is, differing numbers of each subunit type. To adopt this uneven stoichiometry, sequence-identical subunits must be asymmetric with respect to each other, forming different interactions within the complex. Here we first investigate the occurrence of uneven stoichiometry, demonstrating that it is common in vitro and is likely to be common in vivo. Next, we elucidate the structural determinants of uneven stoichiometry, identifying six different mechanisms by which it can be achieved. Finally, we study the frequency of uneven stoichiometry across evolution, observing a significant enrichment in bacteria compared with eukaryotes. We show that this arises due to a general increased tendency for bacterial proteins to self-assemble and form homomeric interactions, even within the context of a heteromeric complex.
- Publication
Nature Communications, 2015, Vol 6, Issue 3, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/ncomms7394