Abstract
Interestingly, some protein domains are intrinsically disordered (abbreviated as IDD), and the disorder degree of same domains may differ in different contexts. However, the evolutionary causes and biological significance of these phenomena are unclear. Here, we address these issues by genome-wide analyses of the evolutionary and functional features of IDDs in 1,870 species across the three superkingdoms. As the result, there is a significant positive correlation between the proportion of IDDs and organism complexity with some interesting exceptions. These phenomena may be due to the high disorder of clade-specific domains and the different disorder degrees of the domains shared in different clades. The functions of IDDs are clade-specific and the higher proportion of post-translational modification sites may contribute to their complex functions. Compared with metazoans, fungi have more IDDs with a consecutive disorder region but a low disorder ratio, which reflects their different functional requirements. As for disorder variation, it’s greater for domains among different proteins than those within the same proteins. Some clade-specific ‘no-variation’ or ‘high-variation’ domains are involved in clade-specific functions. In sum, intrinsic domain disorder is related to both the organism complexity and clade-specific functions. These results deepen the understanding of the evolution and function of IDDs.
Highlights
IntroductionSome protein domains are intrinsically disordered (abbreviated as intrinsically disordered domains (IDDs)), and the disorder degree of same domains may differ in different contexts
Some protein domains are intrinsically disordered, and the disorder degree of same domains may differ in different contexts
In order to achieve a complete representation of the distribution pattern of intrinsically disordered domains (IDDs) across the three superkingdoms, one representative species was chosen from each genus
Summary
Some protein domains are intrinsically disordered (abbreviated as IDD), and the disorder degree of same domains may differ in different contexts. There is a significant positive correlation between the proportion of IDDs and organism complexity with some interesting exceptions These phenomena may be due to the high disorder of clade-specific domains and the different disorder degrees of the domains shared in different clades. Intrinsic domain disorder is related to both the organism complexity and clade-specific functions These results deepen the understanding of the evolution and function of IDDs. Proteins containing intrinsically disordered regions (IDR)[1,2] are called intrinsically disordered proteins (IDP, named as intrinsically u nstructured[3,4] or natively unfolded p roteins5), which haven no stable ordered structure but have important biological functions via interacting with various p artners[1,2,3,6]. Key Laboratory of Environmental and Viral Oncology, College of Life Science and Bioengineering, Beijing University of Technology, Beijing 100124, China. 3These authors contributed : Chao Gao, Chong Ma and Scientific Reports | (2021) 11:2985
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