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Yizhi_et_al-2018-Scientific_Reports.pdf
Preview of Intrinsically Disordered Proteins
🔗 Source: amu.hal.science
📊 Size: 1.75 MB
👤 Author: Yizhi Zhang, Hélène Launay, Antoine Schramm, Régine Lebrun, Brigitte Gontero
⬇️ Downloads: 181

Summary

Researchers identified 682 heat-resistant proteins in Chlamydomonas reinhardtii using mass spectrometry, with 331 of these proteins being targets of phosphorylation. The mean percentage of disorder in these proteins was approximately 20%, with most (~70%) being addressed to compartments other than mitochondrion and chloroplast. The amino acid composition of these proteins was biased, with diverse molecular functions, including nucleic acid binding, unfolded protein binding, and catalytic activity. The most represented proteins were ribosomal proteins, flagella-associated proteins, chaperones, and histones. This study is the first experimental investigation of intrinsically disordered proteins (IDPs) in C. reinhardtii, combining in silico analysis. IDPs are known to play multiple roles in biological processes due to their dynamic properties and flexibility, allowing them to bind a wide range of partners. The study highlights the lack of experimental investigation of IDP content in photosynthetic organisms, despite their high complexity and the importance of IDPs in regulating cellular processes.

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Description

Research on intrinsically disordered proteins in Chlamydomonas reinhardtii. Published in Scientific Reports, 2018. Authors include Yizhi Zhang and Brigitte Gontero.

Technical Information

  • File Format: PDF
  • File Size: 1.75 MB
  • Pages: 12
  • Language: EN
  • Author: Yizhi Zhang, Hélène Launay, Antoine Schramm, Régine Lebrun, Brigitte Gontero
  • Total Downloads: 181
  • Last Updated: 6 days ago

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