Nascent chains derived from a foldable protein sequence interact with specific ribosomal surface sites near the exit tunnel.

ABSTRACT: In order to become bioactive, proteins must be translated and protected from aggregation during biosynthesis. The ribosome and molecular chaperones play a key role in this process. Ribosome-bound nascent chains (RNCs) of intrinsically disordered proteins and RNCs bearing a signal/arrest sequence are known to interact with ribosomal proteins. However, in the case of RNCs bearing foldable protein sequences, not much information is available on these interactions. Here, via a combination of chemical crosslinking and time-resolved fluorescence-anisotropy, we find that nascent chains of the foldable globin apoHmp_1-140 interact with ribosomal protein L23 and have a freely-tumbling non-interacting N-terminal compact region comprising 63-94 residues. Longer RNCs (apoHmp_1-189)

SUBMITTER: Masse MM 

PROVIDER: S-EPMC11137106 | biostudies-literature | 2024 May

REPOSITORIES: biostudies-literature