Summary information and primary citation
- PDB-id
-
8qu5;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- ribosome
- Method
- cryo-EM (2.42 Å)
- Summary
- Mt-lsu assembly intermediate in gtpbp8 knock-out cells,
state 2
- Reference
-
Cipullo M, Valentin Gese G, Gopalakrishna S, Krueger A,
Lobo V, Pirozhkova MA, Marks J, Palenikova P, Shiriaev D,
Liu Y, Misic J, Cai Y, Nguyen MD, Abdelbagi A, Li X,
Minczuk M, Hafner M, Benhalevy D, Sarshad AA, Atanassov
I, Hallberg BM, Rorbach J (2024): "GTPBP8
plays a role in mitoribosome formation in human
mitochondria." Nat Commun,
15, 5664. doi: 10.1038/s41467-024-50011-x.
- Abstract
- Mitochondrial gene expression relies on mitoribosomes
to translate mitochondrial mRNAs. The biogenesis of
mitoribosomes is an intricate process involving multiple
assembly factors. Among these factors, GTP-binding proteins
(GTPBPs) play important roles. In bacterial systems,
numerous GTPBPs are required for ribosome subunit
maturation, with EngB being a GTPBP involved in the
ribosomal large subunit assembly. In this study, we focus
on exploring the function of GTPBP8, the human homolog of
EngB. We find that ablation of GTPBP8 leads to the
inhibition of mitochondrial translation, resulting in
significant impairment of oxidative phosphorylation.
Structural analysis of mitoribosomes from GTPBP8 knock-out
cells shows the accumulation of mitoribosomal large subunit
assembly intermediates that are incapable of forming
functional monosomes. Furthermore, fPAR-CLIP analysis
reveals that GTPBP8 is an RNA-binding protein that
interacts specifically with the mitochondrial ribosome
large subunit 16 S rRNA. Our study highlights the role of
GTPBP8 as a component of the mitochondrial gene expression
machinery involved in mitochondrial large subunit
maturation.
