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  1. Large protein complex interfaces have evolved to promote cotranslational assembly

    This article has 2 authors:
    1. Mihaly Badonyi
    2. Joseph A Marsh
    This article has been curated by 1 group:
    • Curated by eLife

      Evaluation Summary:

      The authors use a combination of proteome-specific protein complex structures and publicly available ribosome profiling data to show that cotranslational assembly is favored by large N-terminal intermolecular interfaces. The manuscript represents an important contribution to the field of protein biosynthesis pathways by suggesting an intuitive evolutionary mechanism that can promote co-translational assembly pathways in mammalians, yeast, and bacteria.

      (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. The reviewers remained anonymous to the authors.)

    Reviewed by eLife

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