Evolutionary Study of Disorder in Protein Sequences
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, w...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-10-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/10/10/1413 |
| _version_ | 1797551619682861056 |
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| author | Kristina Kastano Gábor Erdős Pablo Mier Gregorio Alanis-Lobato Vasilis J. Promponas Zsuzsanna Dosztányi Miguel A. Andrade-Navarro |
| author_facet | Kristina Kastano Gábor Erdős Pablo Mier Gregorio Alanis-Lobato Vasilis J. Promponas Zsuzsanna Dosztányi Miguel A. Andrade-Navarro |
| author_sort | Kristina Kastano |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T15:48:41Z |
| format | Article |
| id | doaj.art-4c1f0cc5f84f4716b084e3aad940f6e0 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T15:48:41Z |
| publishDate | 2020-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-4c1f0cc5f84f4716b084e3aad940f6e02023-11-20T16:14:12ZengMDPI AGBiomolecules2218-273X2020-10-011010141310.3390/biom10101413Evolutionary Study of Disorder in Protein SequencesKristina Kastano0Gábor Erdős1Pablo Mier2Gregorio Alanis-Lobato3Vasilis J. Promponas4Zsuzsanna Dosztányi5Miguel A. Andrade-Navarro6Faculty of Biology, Johannes Gutenberg University, Biozentrum I, Hans-Dieter-Hüsch-Weg 15, 55128 Mainz, GermanyMTA-ELTE Momentum Bioinformatics Research Group, Department of Biochemistry, ELTE Eötvös Loránd University, H-1117 Budapest, HungaryFaculty of Biology, Johannes Gutenberg University, Biozentrum I, Hans-Dieter-Hüsch-Weg 15, 55128 Mainz, GermanyHuman Embryo and Stem Cell Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UKBioinformatics Research Laboratory, Department of Biological Sciences, University of Cyprus, 2109 Nicosia, CyprusMTA-ELTE Momentum Bioinformatics Research Group, Department of Biochemistry, ELTE Eötvös Loránd University, H-1117 Budapest, HungaryFaculty of Biology, Johannes Gutenberg University, Biozentrum I, Hans-Dieter-Hüsch-Weg 15, 55128 Mainz, GermanyIntrinsically 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.https://www.mdpi.com/2218-273X/10/10/1413intrinsically disordered proteinsintrinsically disordered regionscomparative genomicsortholog comparison |
| spellingShingle | Kristina Kastano Gábor Erdős Pablo Mier Gregorio Alanis-Lobato Vasilis J. Promponas Zsuzsanna Dosztányi Miguel A. Andrade-Navarro Evolutionary Study of Disorder in Protein Sequences Biomolecules intrinsically disordered proteins intrinsically disordered regions comparative genomics ortholog comparison |
| title | Evolutionary Study of Disorder in Protein Sequences |
| title_full | Evolutionary Study of Disorder in Protein Sequences |
| title_fullStr | Evolutionary Study of Disorder in Protein Sequences |
| title_full_unstemmed | Evolutionary Study of Disorder in Protein Sequences |
| title_short | Evolutionary Study of Disorder in Protein Sequences |
| title_sort | evolutionary study of disorder in protein sequences |
| topic | intrinsically disordered proteins intrinsically disordered regions comparative genomics ortholog comparison |
| url | https://www.mdpi.com/2218-273X/10/10/1413 |
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