The different roles of the eS31 ribosomal protein in ribosome biogenesis and translation in Saccharomyces cerevisiae

Many ribosomal proteins in yeast possess extensions that protrude from their globular cores to facilitate rRNA folding, ribosome assembly, and translation. Previous work established that the eukaryote-specific N-terminal domain of eS31 harbors a nuclear localization signal; its deletion impairs growth and 40S biogenesis while inducing ribosomal misreading. Gao et al., now provide further insights into this extension, identifying a critical cluster of basic residues essential for elongation fidelity. Furthermore, they demonstrate that full-domain deletion compromises termination through a 'trans-acting disruption' process requiring wild-type eS31. These findings highlight novel mechanisms underlying ribosome heterogeneity and specialization. Comment on: https://doi.org/10.1111/febs.70510.