Pengfei Lan

TL;DR: The nearly complete architecture of Saccharomyces cerevisiae 90S is determined from three cryo-electron microscopy single particle reconstructions at 4.5 to 8.7 angstrom resolution and provides significant insight into the principle of small subunit assembly and the function of assembly factors.

TL;DR: Cryo-electron microscopy structures of the human nuclear RNase P alone and in complex with tRNAVal are reported and an evolutionary model depicting how auxiliary RNA elements in bacterial RN enzyme P, essential for substrate binding, and catalysis, were replaced by the much more complex and multifunctional protein components in higher organisms is provided.

TL;DR: The structure of yeast RNase P in complex with its natural substrate, a tRNA precursor, demonstrates the structural basis for substrate recognition and provides insights into its catalytic mechanism, and high-resolution structures of eukaryotic RNase Ps are reported.

TL;DR: In this article, the authors presented the Cryo-EM structures of human RNA polymerase III in both apo and elongating states, which revealed both an orchestrated movement during the apo-to-elongating transition and an unexpected apo state in which the RPC7 subunit tail occupied the DNA-RNA-binding cleft of Pol III, suggesting that RPC7 plays important roles in both autoinhibition and transcription initiation.

TL;DR: The structures reveal that the subunits of MjaRNase P are strung together to organize the holoenzyme in a dimeric conformation required for efficient catalysis, suggesting a universal catalytic mechanism for all RNase Ps.