A newly published cryo-EM study in EMBO Journal characterized a key step in the process of mitochondrial ribosome formation. The study was led by a team from Science for Life in Sweden.
The team used mitoribosomes from Trypanosoma brucei with reduced RNA and increased protein mass to provide insights into the biogenesis of the mitoribosomal large subunit.
Their analysis revealed that the resulting structure of the assembly factors form a network that spans a distance of 18 nanometres shielding the sensitive ribosomal core that is made of less-stable nucleic acids. The network is designed to connect all the functional regions on the mitoribosomal large subunit for their correlated maturation.
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A phylogenetic analysis further showed that most of the newly identified assembly factors also exist in humans, and therefore the derived characteristics represent general principles. However, an unexpected finding is that some of those factors appeared to lose their activity. Despite being deactivated, they still contribute as structural mediators for a stabilisation of the functionally active partners on the mitoribosomal core. The preservation of the deactivated factors implies a mechanism of the evolutionary conservation of the sequential assembly.
The work showcases how the structural approach of studying stabilized intermediates is instrumental for understanding dynamic macromolecular processes that can be extrapolated to human counterpart metabolic pathways and provide an evolutionary insight.