Ribosomes undergo an unanticipated movement (‘sliding’) while translating homopolymeric A sequences, which provides a biochemical rationale for the observation that iterated AAA codons are under-represented in gene-coding sequences.
Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.
The enzyme that collaborates with ubiquitin ligases to promote the release of defective polypeptides from stalled ribosomes in a process named ribosome-associated degradations has been identified as the ATPase Cdc48.
Comprehensive structural and compositional characterization of the in vivo 30S ribosomal assembly landscape reveals parallel pathways for 3′-domain formation and a previously unknown role for the assembly factor RimP.
The molecular mechanism behind how emetine inhibits the ribosome of the human malaria parasite, along with structural details of the complex formed, is revealed at high resolution using cryo-electron microscopy.
The diffusion coefficients of proteins in the cytoplasm depend on their net charge and the distribution of charge over the protein surface, with positive proteins moving up to 100-fold slower because they bind to ribosomes.