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Structural and evolutionary versatility in protein complexes with uneven stoichiometry

Author

Listed:
  • Joseph A. Marsh

    (MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital
    European Molecular Biology Laboratory, European Bioinformatics Institute)

  • Holly A. Rees

    (European Molecular Biology Laboratory, European Bioinformatics Institute)

  • Sebastian E. Ahnert

    (Theory of Condensed Matter, Cavendish Laboratory, University of Cambridge)

  • Sarah A. Teichmann

    (European Molecular Biology Laboratory, European Bioinformatics Institute
    Theory of Condensed Matter, Cavendish Laboratory, University of Cambridge
    Wellcome Trust Sanger Institute)

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.

Suggested Citation

  • Joseph A. Marsh & Holly A. Rees & Sebastian E. Ahnert & Sarah A. Teichmann, 2015. "Structural and evolutionary versatility in protein complexes with uneven stoichiometry," Nature Communications, Nature, vol. 6(1), pages 1-10, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7394
    DOI: 10.1038/ncomms7394
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    Cited by:

    1. Alexander S Leonard & Sebastian E Ahnert, 2019. "Evolution of interface binding strengths in simplified model of protein quaternary structure," PLOS Computational Biology, Public Library of Science, vol. 15(6), pages 1-15, June.

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