Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii - Archive ouverte HAL Access content directly
Journal Articles Scientific Reports Year : 2018

Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii


The content of intrinsically disordered protein (IDP) is related to organism complexity, evolution, and regulation. In the Plantae, despite their high complexity, experimental investigation of IDP content is lacking. We identified by mass spectrometry 682 heat-resistant proteins from the green alga, Chlamydomonas reinhardtii. Using a phosphoproteome database, we found that 331 of these proteins are targets of phosphorylation. We analyzed the flexibility propensity of the heat-resistant proteins and their specific features as well as those of predicted IDPs from the same organism. Their mean percentage of disorder was about 20%. Most of the IDPs (~70%) were addressed to other compartments than mitochondrion and chloroplast. Their amino acid composition was biased compared to other classic IDPs. Their molecular functions were diverse; the predominant ones were nucleic acid binding and unfolded protein binding and the less abundant one was catalytic activity. The most represented proteins were ribosomal proteins, proteins associated to flagella, chaperones and histones. We also found CP12, the only experimental IDP from C. reinhardtii that is referenced in disordered protein database. This is the first experimental investigation of IDPs in C. reinhardtii that also combines in silico analysis.
Fichier principal
Vignette du fichier
Yizhi_et_al-2018-Scientific_Reports.pdf (1.28 Mo) Télécharger le fichier
Origin Publisher files allowed on an open archive

Dates and versions

hal-01794065 , version 1 (17-05-2018)



Yizhi Zhang, Hélène Launay, Antoine Schramm, Régine Lebrun, Brigitte Gontero. Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii. Scientific Reports, 2018, 8, pp.6805. ⟨10.1038/s41598-018-24772-7⟩. ⟨hal-01794065⟩
302 View
123 Download



Gmail Mastodon Facebook X LinkedIn More