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

In contrast to the other examples, redox-sensitive cysteines in Pet191 are likely to form disulfide bonds when it is located in the intermembrane space of the mitochondria. This protein is a cytochrome c oxidase assembly factor with a similar twin-Cx9C motif, similar to that found in Cox17. The disulfide bond formation is required for cell viability and assembly of the cytochrome c oxidase complex, however the protein may be imported into the mitochondria, independently of the mitochondrial MIA40-ERV1 machinery [47] . This difference could explain why this protein was found to be redox-sensitive, while other members of the COX family were not detected as such. V. Functional repertoire of redox-sensitive structural switches in the human proteome Yeast proteomics results highlight some key molecular mechanisms in which redox-sensitive conditional disorder plays functional roles, most notably in stress response, biogenesis, and the regulation of transcription and translation. These results indicate that these structural switches preferentially contribute to the actuation of certain biological processes. While yeast proteomics can highlight certain functions also present in higher order organisms, biological processes that are unique to higher order multicellular organisms can only be uncovered via the direct analysis of the functional annotations of their proteomes.