A new family of sterol-specific lipid transfer proteins has been found that anchors in the endoplasmic reticulum; some of these proteins stretch across membrane contacts and mediate sterol traffic from the plasma membrane.

The small subunit ribosomal protein uS7/Rps5 interacts with translation initiation factor eIF2α to stabilize first the open, and then the closed conformation of the pre-initiation complex to promote accurate start codon selection in vivo.

A structural element of mRNA exit channel protein Rps5 performs a critical role in start codon recognition during translation initiation by stabilizing initiator tRNA binding to the pre-initiation complex.

The transcription machinery is required for the disassembly of the promoter-proximal H2A.Z nucleosome, contributing to the constitutive histone turnover at yeast promoters.

Examination of the changes in the transcription start site selection in TCL1-driven chronic lymphocytic leukemia and their impact on mRNA translation revealed a marked elevation of intra-genic cryptic promoters, which are predicted to generate multiple N-terminally truncated or modified proteins.

The N-terminal domain (NTD) of the initiation factor eIF5 bound to the 40S subunit at the precise location vacated by eIF1 promotes tRNAi accommodation at AUG codons.

GRAMD1 proteins sense a transient expansion of the accessible pool of plasma membrane cholesterol and facilitate its transport to the endoplasmic reticulum at ER-PM contact sites.

RNA polymerase II generates numerous transcript isoforms, including transcripts initiating downstream of the START codon, that are efficiently degraded by the nonsense-mediated mRNA decay pathway.

In humans, specific sequence features can predict whether meiotic recombination occurs at sites bound by the protein PRDM9, whose DNA-binding zinc-finger domain can unexpectedly bind to gene promoters and to other copies of PRDM9.

Variability in bacterial transcription start site selection involves DNA “scrunching” and “anti-scrunching,” which may represent a general mechanism for start site selection in all organisms.