01794nas a2200193   4500008004100000245015100041210006900192260001300261300001300274490000600287520104500293100002001338700001801358700002801376700002001404700002301424700002301447856013001470       2011                        eng d00aAn evolutionary trade-off between protein turnover rate and protein aggregation favors a higher aggregation propensity in fast degrading proteins.0 aevolutionary tradeoff between protein turnover rate and protein   c2011 Jun  ae10020900 v73 a<p>We previously showed the existence of selective pressure against protein aggregation by the enrichment of aggregation-opposing ’gatekeeper’ residues at strategic places along the sequence of proteins. Here we analyzed the relationship between protein lifetime and protein aggregation by combining experimentally determined turnover rates, expression data, structural data and chaperone interaction data on a set of more than 500 proteins. We find that selective pressure on protein sequences against aggregation is not homogeneous but that short-living proteins on average have a higher aggregation propensity and fewer chaperone interactions than long-living proteins. We also find that short-living proteins are more often associated to deposition diseases. These findings suggest that the efficient degradation of high-turnover proteins is sufficient to preclude aggregation, but also that factors that inhibit proteasomal activity, such as physiological ageing, will primarily affect the aggregation of short-living proteins.</p>1 aDe Baets, Greet1 aReumers, Joke1 aBlanco, Javier, Delgado1 aDopazo, Joaquin1 aSchymkowitz, Joost1 aRousseau, Frederic  uhttps://www.clinbioinfosspa.es/content/evolutionary-trade-between-protein-turnover-rate-and-protein-aggregation-favors-higher