Cotranslational assembly of protein complexes in eukaryotes revealed by ribosome profiling.

ABSTRACT: The folding of newly synthesized proteins to the native state is a major challenge within the crowded cellular environment, as non-productive interactions can lead to misfolding, aggregation and degradation¹. Cells cope with this challenge by coupling synthesis with polypeptide folding and by using molecular chaperones to safeguard folding cotranslationally². However, although most of the cellular proteome forms oligomeric assemblies³, little is known about the final step of folding: the assembly of polypeptides into complexes. In prokaryotes, a proof-of-concept study showed that the assembly of heterodimeric luciferase is an organized cotranslational process that is facilitated by spatially confined translation of the subunits encoded on a polycistronic mR

SUBMITTER: Shiber A 

PROVIDER: S-EPMC6372068 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature