Protein Abundance Biases the Amino Acid Composition of Disordered Regions to Minimize Non-functional Interactions.

ABSTRACT: In eukaryotes, disordered regions cover up to 50% of proteomes and mediate fundamental cellular processes. In contrast to globular domains, where about half of the amino acids are buried in the protein interior, disordered regions show higher solvent accessibility, which makes them prone to engage in non-functional interactions. Such interactions are exacerbated by the law of mass action, prompting the question of how they are minimized in abundant proteins. We find that interaction propensity or "stickiness" of disordered regions negatively correlates with their cellular abundance, both in yeast and human. Strikingly, considering yeast proteins where a large fraction of the sequence is disordered, the correlation between stickiness and abundance reaches R=-0.55. Beyond this global amino-a

SUBMITTER: Dubreuil B 

PROVIDER: S-EPMC6941228 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature