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Emergence and evolution of an interaction between intrinsically disordered proteins
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Number of Authors: 9
2017 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 6, e16059Article in journal (Refereed) Published
Abstract [en]

Protein-protein interactions involving intrinsically disordered proteins are important for cellular function and common in all organisms. However, it is not clear how such interactions emerge and evolve on a molecular level. We performed phylogenetic reconstruction, resurrection and biophysical characterization of two interacting disordered protein domains, CID and NCBD. CID appeared after the divergence of protostomes and deuterostomes 450-600 million years ago, while NCBD was present in the protostome/deuterostome ancestor. The most ancient CID/NCBD formed a relatively weak complex (K(d similar to)5 mu M). At the time of the first vertebrate-specific whole genome duplication, the affinity had increased (K-d\similar to 200 nM) and was maintained in further speciation. Experiments together with molecular modeling using NMR chemical shifts suggest that new interactions involving intrinsically disordered proteins may evolve via a low-affinity complex which is optimized by modulating direct interactions as well as dynamics, while tolerating several potentially disruptive mutations.

Place, publisher, year, edition, pages
2017. Vol. 6, e16059
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Biological Sciences
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URN: urn:nbn:se:su:diva-143592DOI: 10.7554/eLife.16059ISI: 000400663100001OAI: oai:DiVA.org:su-143592DiVA: diva2:1104086
Available from: 2017-05-31 Created: 2017-05-31 Last updated: 2017-05-31Bibliographically approved

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Dogan, Jakob
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Department of Biochemistry and Biophysics
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