Journal
TRENDS IN CELL BIOLOGY
Volume 31, Issue 4, Pages 284-297Publisher
CELL PRESS
DOI: 10.1016/j.tcb.2020.12.008
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Funding
- National Institute of General Medical Sciences (NIGMS)-MIRA (Maximizing Investigators' Research Award) [R35GM118141]
- Muscular Dystrophy Association Research Grant [MDA-381828]
- American Heart Association postdoctoral fellowship [19POST34450174]
- Deutsche Forschungsgemeinschaft by the Emmy-Noether grant [RI 2715/1-1]
- Deutsche Forschungsgemeinschaft by the Excellence Cluster [EXC 2067/1-390729940]
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This review summarizes recent progress in the understanding of mitoribosome assembly GTPases, describing their features, mechanisms of action, and possible roles in the formation of mitoribosomal subunits. The authors also propose a unified nomenclature for mitoribosome assembly GTPases following the recent nomenclature unification for mitoribosomal proteins.
Mitoribosomes catalyze essential protein synthesis within mitochondria. Mitoribosome biogenesis is assisted by an increasing number of assembly factors, among which guanosine triphosphate hydrolases (GTPases) are the most abundant class. Here, we review recent progress in our understanding of mitoribosome assembly GTPases. We describe their shared and specific features and mechanisms of action, compare them with their bacterial counterparts, and discuss their possible roles in the assembly of small or large mitoribosomal subunits and the formation of the monosome by establishing quality-control checkpoints during these processes. Furthermore, following the recent unification of the nomenclature for the mitoribosomal proteins, we also propose a unified nomenclature for mitoribosome assembly GTPases.
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