A functional connection between translation elongation and protein folding at the ribosome exit tunnel in Saccharomyces cerevisiae.

ABSTRACT: Proteostasis needs to be tightly controlled to meet the cellular demand for correctly de novo folded proteins and to avoid protein aggregation. While a coupling between translation rate and co-translational folding, likely involving an interplay between the ribosome and its associated chaperones, clearly appears to exist, the underlying mechanisms and the contribution of ribosomal proteins remain to be explored. The ribosomal protein uL3 contains a long internal loop whose tip region is in close proximity to the ribosomal peptidyl transferase center. Intriguingly, the rpl3[W255C] allele, in which the residue making the closest contact to this catalytic site is mutated, affects diverse aspects of ribosome biogenesis and function. Here, we have uncovered, by performing a synthetic lethal scr

SUBMITTER: Rodriguez-Galan O 

PROVIDER: S-EPMC7797049 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature