Large-scale analysis of redox-sensitive conditionally disordered protein regions reveal their widespread nature and key roles in high-level eukaryotic processes

Gábor Erdos; Bálint Mészáros; Dana Reichmann; Zsuzsanna Dosztányi

Molecular level functions highlight that the dominant processes uncovered by yeast proteomics are also heavily associated with redox-sensitive conditional disorder in the human proteome. These processes are linked to the regulation of transcription and translation, and are dominated by intracellular proteins. Consequently, the corresponding GO terms are clearly linked to metal ion coordinating regions. In addition, these structural elements are also associated with the biosynthesis of several organic compounds, processes that are largely absent from the results of yeast proteomics. While corresponding processes do exist in yeast, they involve only a very limited number of proteins in contrast to the similar function in humans (e.g. 'nucleobasecontaining compound metabolic process' covering only 7 yeast proteins [48] ). A separate class of GO molecular slim terms correspond to the multicellular-specific metabolism and organization of the extracellular matrix in general, and collagen fibrils in particular. These processes are clearly dominated by extracellular proteins, and are thus strongly associated with redoxsensitive disulfide bridge forming protein regions.