Extensive molecular profiling shows how loss of highly similar, paralogous ribosomal proteins lead to distinct phenotypic outputs, through translational control of specific mRNAs.

Ribosomal proteins Rps27 (eS27) and Rps27l (eS27L) are an ancient pair of duplicated genes that encode functionally interchangeable proteins, yet have been evolutionarily retained because both copies are necessary to achieve protein expression across cell types.

A novel co-translational mechanism continuously adjusts the expression levels of ribosomal proteins Rpl3 and Rpl4 to their consumption during ribosome synthesis by regulating the abundance of their mRNAs.

Tom1 is the ubiquitin ligase in yeast that anchors a protein quality control pathway that rapidly eliminates ribosomal proteins that fail to assemble into ribosomes.

The ribosomal protein, Rps27l, plays an oncogenic role by promoting p53 degradation via stabilizing the Mdm2-Mdm4 complex, but a tumor suppressor role by preventing the aneuploidy and loss of p53 heterozygosity.

The ATPase Fap7 prefabricates a uS11:eS26 ribosomal protein complex for ribosome assembly.

Asc1/RACK1 promotes the translation of mRNAs associated with the translational closed loop complex, which have short open reading frames and encode proteins required for core metabolic processes.

Cell competition is an important mechanism selecting against aneuploid cells.

The messenger RNA encoding La-related protein-4 (LARP4) contains a short region of instability whose codon clusters are sensitive to low abundance tRNAs that when elevated increase LARP4 activity for poly(A) lengthening of ribosomal protein mRNAs and other mRNAs.

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.