Martin Saurer

TL;DR: The atomic structure of the chloroplast 70S ribosome prepared from spinach leaves and resolved by cryo‐EM at 3.4 Å resolution reveals the features of the 4.5S rRNA, which probably evolved by the fragmentation of the 23S r RNA, and all five plastid‐specific ribosomal proteins.

TL;DR: The assembly of the small mitoribosomal subunit in Trypanosoma brucei involves a large number of factors and proceeds through the formation of assembly intermediates, which are analyzed by using cryo–electron microscopy.

TL;DR: The structural basis of mammalian ribosome assembly is not well understood as mentioned in this paper, but it has been shown that the NSUN4-MTERF4 dimer plays a critical role in the process by stabilizing the 16S rRNA in a conformation that exposes the functionally important regions of rRNA for modification by the MRM2 methyltransferase and quality control interactions with the conserved mitochondrial GTPase MTG2 that contacts the sarcin-ricin loop and the immature active site.

TL;DR: It is discovered that mitochondrial initiation factor 2 participates in the assembly of the small mitoribosomal subunit from Trypanosoma brucei, and that modular exchange of ribosomal proteins and assembly factors together with mt-IF-2 ensure proper 9S rRNA folding and protein maturation during the final steps of assembly.

TL;DR: The structure of the mammalian mitochondrial ribosome assembly is not understood as discussed by the authors, but it has been shown that NSUN4-MTERF4 dimer plays a critical role in the process by stabilizing the 16S rRNA in a conformation that exposes the functionally important regions of rRNA for modification by MRM2 methyltransferase and quality control interactions with a conserved mitochondrial GTPase MTG2.