Microbial cells optimally structure their proteomes in order to mutually maximize metabolism and translation, as established by an extensive comparison between data and a low-dimensional model of cellular physiology.

Live-cell imaging, genetic analysis and electron cryomicroscopy identify structural motifs involved in the differential assembly of Pol I-Rrn3 complexes and Pol I homodimers in response to nutrient availability.

Embryonic development requires autophagy-dependent degradation of ribosomal RNAs.

A pattern recognition receptor called toll-like receptor 13 detects pathogens in a manner that is different to that seen in other pathogen sensors.

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.

RNA-level regulation of gene expression is negatively associated with protein-level regulation across cellular pathways in normal tissues and cancer.

Local presynaptic protein synthesis occurring at established nerve terminals in the mammalian brain provides a mechanism for rapidly controlling or restoring presynaptic proteins that affect neurotransmitter release and presynaptic efficiency.

Global relative mRNA and protein abundance in trypanosomatids can be effectively estimated at transcriptomic and proteomic scales based on protein-coding sequences alone.

Brain region-specific profiling of O-GlcNAcylation interactome in Drosophila mushroom body suggests that hypo-O-GlcNAcylation impacts cognitive function by regulating translational activity.

A near-complete flux balance analysis model of a minimal cell demonstrates the high essentiality of its metabolic genes, agrees well with experimental essentiality data and suggests some further gene removals.