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Evolutionary Study of Disorder in Protein Sequences

Faculty of Biology, Johannes Gutenberg University, Biozentrum I, Hans-Dieter-Hüsch-Weg 15, 55128 Mainz, Germany
MTA-ELTE Momentum Bioinformatics Research Group, Department of Biochemistry, ELTE Eötvös Loránd University, H-1117 Budapest, Hungary
Human Embryo and Stem Cell Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK
Bioinformatics Research Laboratory, Department of Biological Sciences, University of Cyprus, 2109 Nicosia, Cyprus
Author to whom correspondence should be addressed.
Biomolecules 2020, 10(10), 1413;
Received: 2 September 2020 / Revised: 29 September 2020 / Accepted: 3 October 2020 / Published: 6 October 2020
(This article belongs to the Special Issue Computational Perspectives on Intrinsic Disorder-Based Functionality)
Intrinsically disordered proteins (IDPs) contain regions lacking intrinsic globular structure (intrinsically disordered regions, IDRs). IDPs are present across the tree of life, with great variability of IDR type and frequency even between closely related taxa. To investigate the function of IDRs, we evaluated and compared the distribution of disorder content in 10,695 reference proteomes, confirming its high variability and finding certain correlation along the Euteleostomi (bony vertebrates) lineage to number of cell types. We used the comparison of orthologs to study the function of disorder related to increase in cell types, observing that multiple interacting subunits of protein complexes might gain IDRs in evolution, thus stressing the function of IDRs in modulating protein-protein interactions, particularly in the cell nucleus. Interestingly, the conservation of local compositional biases of IDPs follows residue-type specific patterns, with E- and K-rich regions being evolutionarily stable and Q- and A-rich regions being more dynamic. We provide a framework for targeted evolutionary studies of the emergence of IDRs. We believe that, given the large variability of IDR distributions in different species, studies using this evolutionary perspective are required. View Full-Text
Keywords: intrinsically disordered proteins; intrinsically disordered regions; comparative genomics; ortholog comparison intrinsically disordered proteins; intrinsically disordered regions; comparative genomics; ortholog comparison
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MDPI and ACS Style

Kastano, K.; Erdős, G.; Mier, P.; Alanis-Lobato, G.; Promponas, V.J.; Dosztányi, Z.; Andrade-Navarro, M.A. Evolutionary Study of Disorder in Protein Sequences. Biomolecules 2020, 10, 1413.

AMA Style

Kastano K, Erdős G, Mier P, Alanis-Lobato G, Promponas VJ, Dosztányi Z, Andrade-Navarro MA. Evolutionary Study of Disorder in Protein Sequences. Biomolecules. 2020; 10(10):1413.

Chicago/Turabian Style

Kastano, Kristina, Gábor Erdős, Pablo Mier, Gregorio Alanis-Lobato, Vasilis J. Promponas, Zsuzsanna Dosztányi, and Miguel A. Andrade-Navarro. 2020. "Evolutionary Study of Disorder in Protein Sequences" Biomolecules 10, no. 10: 1413.

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