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Open AccessArticle

In Silico Analysis of Correlations between Protein Disorder and Post-Translational Modifications in Algae

RIKEN Center for Sustainable Resource Science, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan
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Academic Editors: Lukasz Kurgan and Vladimir N. Uversky
Int. J. Mol. Sci. 2015, 16(8), 19812-19835; https://doi.org/10.3390/ijms160819812
Received: 29 May 2015 / Revised: 12 August 2015 / Accepted: 13 August 2015 / Published: 20 August 2015
Recent proteome analyses have reported that intrinsically disordered regions (IDRs) of proteins play important roles in biological processes. In higher plants whose genomes have been sequenced, the correlation between IDRs and post-translational modifications (PTMs) has been reported. The genomes of various eukaryotic algae as common ancestors of plants have also been sequenced. However, no analysis of the relationship to protein properties such as structure and PTMs in algae has been reported. Here, we describe correlations between IDR content and the number of PTM sites for phosphorylation, glycosylation, and ubiquitination, and between IDR content and regions rich in proline, glutamic acid, serine, and threonine (PEST) and transmembrane helices in the sequences of 20 algae proteomes. Phosphorylation, O-glycosylation, ubiquitination, and PEST preferentially occurred in disordered regions. In contrast, transmembrane helices were favored in ordered regions. N-glycosylation tended to occur in ordered regions in most of the studied algae; however, it correlated positively with disordered protein content in diatoms. Additionally, we observed that disordered protein content and the number of PTM sites were significantly increased in the species-specific protein clusters compared to common protein clusters among the algae. Moreover, there were specific relationships between IDRs and PTMs among the algae from different groups. View Full-Text
Keywords: algae; glycosylation; protein disorder; post-translational modifications; phosphorylation; ubiquitination algae; glycosylation; protein disorder; post-translational modifications; phosphorylation; ubiquitination
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Kurotani, A.; Sakurai, T. In Silico Analysis of Correlations between Protein Disorder and Post-Translational Modifications in Algae. Int. J. Mol. Sci. 2015, 16, 19812-19835.

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