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Updated: May 4, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Correlations between predicted protein disorder and post-translational modifications in plants
Atsushi Kurotani1, Alexander A Tokmakov2, Yutaka Kuroda2
1RIKEN Center for Sustainable Resource Science 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan, Department of Biotechnology and Life Science, Faculty of Technology, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan and Research Center for Environmental Genomics, Kobe University, 1-1 Rokko dai, Nada, Kobe 657-8501, Japan RIKEN Center for Sustainable Resource Science 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan, Department of Biotechnology and Life Science, Faculty of Technology, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan and Research Center for Environmental Genomics, Kobe University, 1-1 Rokko dai, Nada, Kobe 657-8501, Japan.
This study reveals plant protein disorder correlates with post-translational modifications (PTMs). Phosphorylation and glycosylation favor disordered regions, while methylation avoids them, highlighting differences between monocots and dicots.
Area of Science:
- Plant molecular biology
- Proteomics
- Structural biology
Background:
- Plant protein structural research lags behind animal and bacterial systems.
- Systematic studies on plant protein disorder and multiple post-translational modifications (PTMs) are lacking.
Purpose of the Study:
- To investigate the relationship between intrinsic protein disorder and multiple PTMs across plant proteomes.
- To compare these relationships in monocotyledonous and dicotyledonous plant species.
Main Methods:
- Calculated the degree of intrinsic disorder for complete proteomes of eight plant species.
- Predicted sites for phosphorylation, glycosylation, acetylation, and methylation.
- Examined correlations between protein disorder and predicted PTM sites.
Main Results:
- Phosphorylation, acetylation, and O-glycosylation preferentially occur in disordered regions.
- Methylation tends to avoid disordered regions; N-glycosylation shows no universal preference.
- Monocot proteomes exhibit higher disorder, O-glycosylation, and R-methylation rates compared to dicots.
- Monocots show lower N-glycosylation, K-acetylation, and K-methylation rates than dicots.
Conclusions:
- Protein disorder is significantly linked to multiple PTMs in plants.
- Distinct proteome characteristics exist between monocotyledonous and dicotyledonous species regarding protein disorder and PTMs.
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