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Emergence and evolution of an interaction between intrinsically disordered proteins
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 char...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5419745/ https://www.ncbi.nlm.nih.gov/pubmed/28398197 http://dx.doi.org/10.7554/eLife.16059 |
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author | Hultqvist, Greta Åberg, Emma Camilloni, Carlo Sundell, Gustav N Andersson, Eva Dogan, Jakob Chi, Celestine N Vendruscolo, Michele Jemth, Per |
author_facet | Hultqvist, Greta Åberg, Emma Camilloni, Carlo Sundell, Gustav N Andersson, Eva Dogan, Jakob Chi, Celestine N Vendruscolo, Michele Jemth, Per |
author_sort | Hultqvist, Greta |
collection | PubMed |
description | 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)∼5 µM). At the time of the first vertebrate-specific whole genome duplication, the affinity had increased (K(d)∼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. DOI: http://dx.doi.org/10.7554/eLife.16059.001 |
format | Online Article Text |
id | pubmed-5419745 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-54197452017-05-08 Emergence and evolution of an interaction between intrinsically disordered proteins Hultqvist, Greta Åberg, Emma Camilloni, Carlo Sundell, Gustav N Andersson, Eva Dogan, Jakob Chi, Celestine N Vendruscolo, Michele Jemth, Per eLife Biophysics and Structural Biology 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)∼5 µM). At the time of the first vertebrate-specific whole genome duplication, the affinity had increased (K(d)∼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. DOI: http://dx.doi.org/10.7554/eLife.16059.001 eLife Sciences Publications, Ltd 2017-04-11 /pmc/articles/PMC5419745/ /pubmed/28398197 http://dx.doi.org/10.7554/eLife.16059 Text en © 2017, Hultqvist et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Biophysics and Structural Biology Hultqvist, Greta Åberg, Emma Camilloni, Carlo Sundell, Gustav N Andersson, Eva Dogan, Jakob Chi, Celestine N Vendruscolo, Michele Jemth, Per Emergence and evolution of an interaction between intrinsically disordered proteins |
title | Emergence and evolution of an interaction between intrinsically disordered proteins |
title_full | Emergence and evolution of an interaction between intrinsically disordered proteins |
title_fullStr | Emergence and evolution of an interaction between intrinsically disordered proteins |
title_full_unstemmed | Emergence and evolution of an interaction between intrinsically disordered proteins |
title_short | Emergence and evolution of an interaction between intrinsically disordered proteins |
title_sort | emergence and evolution of an interaction between intrinsically disordered proteins |
topic | Biophysics and Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5419745/ https://www.ncbi.nlm.nih.gov/pubmed/28398197 http://dx.doi.org/10.7554/eLife.16059 |
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