Structures of the signal recognition particle before and after it captures a transmembrane domain suggest how it chooses, engages, and shields its clients during membrane protein targeting to the endoplasmic reticulum.

The signal recognition particle only stably engages translating ribosome nascent-chain complexes exposing a functional signal sequence.

Archaea can contain permuted versions of the universal signal recognition particle RNA, which require a moonlighting activity of the tRNA splicing machinery to generate functional circular RNAs.

Ire1α co-opts the Sec61 translocon channel to efficiently cleave its mRNA substrates during endoplasmic reticulum stress conditions.

Single molecule microscopy combined with biochemical analyses show that a two-step lipid-binding mechanism of the SRP receptor balances the trade-off between speed and specificity during co-translational protein targeting.

Initiation of the assembly of HIV-1 particles in infected cells is required to form a subviral structure that recognizes the viral RNA genome for packaging.

METRIS is a method that reports a mechanical readout of protein-protein interactions and due to its unique properties, it will allow many protein-protein interactions to be quantitatively measured easily that are currently laborious to measure with conventional methods.

Transcriptome-scale RNA imaging and lifetime measurements reveal that the E. coli transcriptome is spatially organized and that this organization modulates the post-transcriptional fate of bacterial mRNAs.

Translation pauses occur in strategic positions to facilitate the production of properly folded membrane proteins in bacteria.