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Structure paper

TitleGTPBP8 plays a role in mitoribosome formation in human mitochondria.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 5664, Year 2024
Publish dateJul 5, 2024
AuthorsMiriam Cipullo / Genís Valentín Gesé / Shreekara Gopalakrishna / Annika Krueger / Vivian Lobo / Maria A Pirozhkova / James Marks / Petra Páleníková / Dmitrii Shiriaev / Yong Liu / Jelena Misic / Yu Cai / Minh Duc Nguyen / Abubakar Abdelbagi / Xinping Li / Michal Minczuk / Markus Hafner / Daniel Benhalevy / Aishe A Sarshad / Ilian Atanassov / B Martin Hällberg / Joanna Rorbach /
PubMed AbstractMitochondrial gene expression relies on mitoribosomes to translate mitochondrial mRNAs. The biogenesis of mitoribosomes is an intricate process involving multiple assembly factors. Among these ...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.
External linksNat Commun / PubMed:38969660 / PubMed Central
MethodsEM (single particle)
Resolution2.42 - 6.75 Å
Structure data

18438

8qrk

EMDB-18438, PDB-8qrk:
mt-SSU assembly intermediate in GTPBP8 knock-out cells, state 1
Method: EM (single particle) / Resolution: 6.75 Å

18439

8qrl

EMDB-18439, PDB-8qrl:
mt-SSU assembly intermediate in GTPBP8 knock-out cells, state 2
Method: EM (single particle) / Resolution: 3.96 Å

18440

8qrm

EMDB-18440, PDB-8qrm:
mt-SSU assembly intermediate in GTPBP8 knock-out cells, state 3
Method: EM (single particle) / Resolution: 3.05 Å

18443

8qrn

EMDB-18443: mt-SSU assembly intermediate in GTPBP8 knock-out cells, state 4
PDB-8qrn: mt-SSU in GTPBP8 knock-out cells, state 4
Method: EM (single particle) / Resolution: 2.98 Å

18460

8qu1

EMDB-18460, PDB-8qu1:
mt-LSU assembly intermediate in GTPBP8 knock-out cells, state 1
Method: EM (single particle) / Resolution: 2.74 Å

18461

8qu5

EMDB-18461, PDB-8qu5:
mt-LSU assembly intermediate in GTPBP8 knock-out cells, state 2
Method: EM (single particle) / Resolution: 2.42 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-SPM:
SPERMINE

ChemComp-SRY:
STREPTOMYCIN / medication, antibiotic*YM

ChemComp-K:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-GNP:
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GppNHp, GMPPNP, energy-carrying molecule analogue*YM

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-HOH:
WATER

ChemComp-FME:
N-FORMYLMETHIONINE

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-PNS:
4'-PHOSPHOPANTETHEINE

Source
  • homo sapiens (human)
KeywordsRIBOSOME / Mitochondria / Assembly / GTPBP8

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