ArticleProceedings of the National Academy of Sciences of the United States of America2017
Evolutionary diversification of protein-protein interactions by interface add-ons.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Engineered kin recognition specificities in the TraA cell surface receptor.The ISME journal · 2026Article
- Activity Regulation of a Glutamine Amidotransferase Bienzyme Complex by Substrate-Induced Subunit Interface Expansion.ACS catalysis · 2025Article
- Validation of aminodeoxychorismate synthase and anthranilate synthase as novel targets for bispecific antibiotics inhibiting conserved protein-protein interactions.Applied and environmental microbiology · 2024Article
- Designing Cyclic-Constrained Peptides to Inhibit Human Phosphoglycerate Dehydrogenase.Molecules (Basel, Switzerland) · 2023Article
- How gene duplication diversifies the landscape of protein oligomeric state and function.Current opinion in genetics & development · 2022Review
- Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing.Nature chemical biology · 2021Article
- An improved statistical method to identify chemical-genetic interactions by exploiting concentration-dependence.PloS one · 2021Article
- Conserved genomic neighborhood is a strong but no perfect indicator for a direct interaction of microbial gene products.BMC bioinformatics · 2020Article
- Article
- 'Democratized' genomic enzymology web tools for functional assignment.Current opinion in chemical biology · 2018Review
- Characteristics of a PHD Finger Subtype.Biochemistry · 2018Article
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Authors and funding
8 authors.
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Abstract
Cells contain a multitude of protein complexes whose subunits interact with high specificity. However, the number of different protein folds and interface geometries found in nature is limited. This raises the question of how protein-protein interaction specificity is achieved on the structural level and how the formation of nonphysiological complexes is avoided. Here, we describe structural elements called interface add-ons that fulfill this function and elucidate their role for the diversification of protein-protein interactions during evolution. We identified interface add-ons in 10% of a representative set of bacterial, heteromeric protein complexes. The importance of interface add-ons for protein-protein interaction specificity is demonstrated by an exemplary experimental characterization of over 30 cognate and hybrid glutamine amidotransferase complexes in combination with comprehensive genetic profiling and protein design. Moreover, growth experiments showed that the lack of interface add-ons can lead to physiologically harmful cross-talk between essential biosynthetic pathways. In sum, our complementary in silico, in vitro, and in vivo analysis argues that interface add-ons are a practical and widespread evolutionary strategy to prevent the formation of nonphysiological complexes by specializing protein-protein interactions.
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