In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteome.

ABSTRACT: A question of fundamental importance concerning protein folding in vivo is whether the kinetics of translation or the thermodynamics of the ribosome nascent chain (RNC) complex is the major determinant of cotranslational folding behavior. This is because translation rates can reduce the probability of cotranslational folding below that associated with arrested ribosomes, whose behavior is determined by the equilibrium thermodynamics of the RNC complex. Here, we combine a chemical kinetic equation with genomic and proteomic data to predict domain folding probabilities as a function of nascent chain length for Escherichia coli cytosolic proteins synthesized on both arrested and continuously translating ribosomes. Our results indicate that, at in vivo translation rates, about one-third of the

SUBMITTER: Ciryam P 

PROVIDER: S-EPMC3545769 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature