Quantifying chaperone-mediated transitions in the proteostasis network of E. coli.

ABSTRACT: For cells to function, the concentrations of all proteins in the cell must be maintained at the proper levels (proteostasis). This task--complicated by cellular stresses, protein misfolding, aggregation, and degradation--is performed by a collection of chaperones that alter the configurational landscape of a given client protein through the formation of protein-chaperone complexes. The set of all such complexes and the transitions between them form the proteostasis network. Recently, a computational model was introduced (FoldEco) that synthesizes experimental data into a system-wide description of the proteostasis network of E. coli. This model describes the concentrations over time of all the species in the system, which include different conformations of the client protein, as well as pr

SUBMITTER: Dickson A 

PROVIDER: S-EPMC3828153 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature