Author:
Forcelloni Sergio,Giansanti Andrea
Abstract
AbstractIn this study, we analyze the role of different structural variants of proteins in the speciation processes. We separate human and mouse proteomes (taken as a reference) into three previously defined variants of disorder: ordered proteins (ORDPs), structured proteins with intrinsically disordered protein regions (IDPRs), and intrinsically disordered proteins (IDPs). Then, using the representation we call here Forsdyke plot, we study the correlation of DNA divergence with the corresponding protein (phenotypic) divergence in the three variants, comparing human and mouse coding sequences with their homologs from 26 eukaryotes. The parameters of the correlation are related to the speciation process. We find that the three variants of disordered proteins are differently related to the speciation process. Specifically, IDPs phenotypically diverge earlier than ORDPs and IDPRs. ORDPs diverge later but are phenotypically more reactive to nucleotide mutations than IDPRs and IDPs. Finally, IDPRs appear to diverge phenotypically later than IDPs, like ORDPs, but they are prone to accept mutations with rates that are similar to those of IDPs. We conclude that IDPs are involved in the early stages of the speciation process, whereas mutations in ORDPs, once speciation is initiated, accelerate phenotypic divergence.
Publisher
Springer Science and Business Media LLC
Reference27 articles.
1. Forsdyke, D. R. When acting as a reproductive barrier for sympatric speciation, hybrid sterility can only be primary. Biological Journal of the Linnean Society XX, 1–10 (2019).
2. Darling, A. L. & Uversky, V. N. Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter. Front. Genet. 4, 9–158 (2018).
3. Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F. & Jones, D. T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol. 337, 635–45 (2004).
4. Uversky, V. N. Functional roles of transiently and intrinsically disordered regions within proteins. FEBS Journal 282, 1182–1189 (2015).
5. Tokuriki, N. & Tawfik, D. S. Protein Dynamism and Evolvability. Science 324, 203–7 (2009).
Cited by
13 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献