A feature analysis of lower solubility proteins in three eukaryotic systems.

摘要: Abstract Because misfolded and damaged proteins can form potentially harmful aggregates, all living organisms have evolved a wide variety of quality control mechanisms. However, the timely clearance aggregation-prone species may not always be achieved, leading to accumulation low solubility proteins. At same time, promiscuity, which driving force for aggregation, is also important functionality certain large number interaction partners. Considerable efforts been made towards characterizing why some appear more than others. In this study, we analyze features precipitate following centrifugation in unstressed yeast cells, human SH-SY5Y cells mouse brain tissue. By normalizing protein abundance, devised an approach whereby lower are reliably identified. Our findings indicate that these tend longer, abundance proteins, contain fewer hydrophobic amino acids. Furthermore, complexity disordered regions. Overall, observed increase link functional aggregates. results from three biologically distinct model systems share several common traits, shedding light on universal determinants. Biological significance We set up novel identify by comparing precipitated with those remain soluble after centrifugation. analyzing eukaryotic parallel, were able traits cross barrier, as well species-specific characteristics. Notably, our analyses revealed primary secondary structural apart connected them greater potential promiscuity. This article part Special Issue entitled: Protein dynamics health disease. Guest Editors: Pierre Thibault Anne-Claude Gingras.