The novel cryo-electron microscopy structure of a bacterial protein-only RNase P illustrates how a small protein oligomerizes into a dodecameric assembly to catalyze the 5’-end maturation of tRNAs.

Solid state NMR is unable to detect any association of substrate to the second binding site, S2, in the extracellular vestibule of the Neurotransmitter:Sodium Symporter LeuT.

Analysis of the Escherichia coli DnaB helicase•bacteriophage λ helicase loader (λP) complex provides insights into helicase opening, delivery to the origin and ssDNA entry, and closing in preparation for translocation.

A phage-encoded protein inhibits a bacterial replicative helicase loading factor by exploiting an internal site that auto-regulates loader self-assembly and ATPase activity.

Par3 is polarized in the plane of the vertebrate neural plate, binds and recruits Prickle3 to the apical membrane and promotes the formation of core planar cell polarity complexes.

Potassium presumably binds to the Na1 site in LeuT, playing a role in inwardly rectifying the transport of substrates.

Many bacteria use the Nus factor antitermination complex to prevent premature Rho-dependent transcription termination of their CRISPR arrays.

NusG enhances transcription elongation by stabilizing DNA base pairs immediately upstream of the RNA-DNA hybrid but does not measurably affect the nucleotide incorporation and the forward translocation by RNA polymerase.

Differences in HDR product preference present a novel mechanism in plants to control substrate availability for short- and long-chain isoprenoids.