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The length scale of multivalent interactions is evolutionarily conserved in fungal and vertebrate phase-separating proteins

Pouria Dasmeh, Roman Doronin, Andreas Wagner
doi: https://doi.org/10.1101/2021.05.04.442641
Pouria Dasmeh
1Institute for Evolutionary Biology and Environmental Studies, University of Zurich, Zurich, Switzerland
3Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA USA 02139
4Swiss Institute of Bioinformatics (SIB)
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  • For correspondence: p.dasmeh@gmail.com
Roman Doronin
1Institute for Evolutionary Biology and Environmental Studies, University of Zurich, Zurich, Switzerland
4Swiss Institute of Bioinformatics (SIB)
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Andreas Wagner
1Institute for Evolutionary Biology and Environmental Studies, University of Zurich, Zurich, Switzerland
2The Santa Fe Institute, Santa Fe, New Mexico
4Swiss Institute of Bioinformatics (SIB)
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Abstract

One key feature of proteins that form liquid droplets by phase separation inside a cell is the presence of multiple sites – multivalency – that mediate interactions with other proteins. We know little about the variation of multivalency on evolutionary time scales. Here, we investigated the long-term evolution (∼600 million years) of multivalency in fungal mRNA decapping subunit 2 protein (Dcp2), and in the FET protein family. We found that multivalency varies substantially among the orthologs of these proteins. However, evolution has maintained the length scale at which sequence motifs that enable protein-protein interactions occur. That is, the total number of such motifs per hundred amino acids is higher and less variable than expected by neutral evolution. To help explain this evolutionary conservation, we developed a conformation classifier using machine-learning algorithms. This classifier demonstrates that disordered segments in Dcp2 and FET proteins tend to adopt compact conformations, which is necessary for phase separation. Thus, the evolutionary conservation we detected may help proteins preserve the ability to undergo phase separation. Altogether, our study reveals that the length scale of multivalent interactions is an evolutionarily conserved feature of two classes of phase-separating proteins in fungi and vertebrates.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted May 04, 2021.
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The length scale of multivalent interactions is evolutionarily conserved in fungal and vertebrate phase-separating proteins
Pouria Dasmeh, Roman Doronin, Andreas Wagner
bioRxiv 2021.05.04.442641; doi: https://doi.org/10.1101/2021.05.04.442641
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The length scale of multivalent interactions is evolutionarily conserved in fungal and vertebrate phase-separating proteins
Pouria Dasmeh, Roman Doronin, Andreas Wagner
bioRxiv 2021.05.04.442641; doi: https://doi.org/10.1101/2021.05.04.442641

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