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TitleA late-stage assembly checkpoint of the human mitochondrial ribosome large subunit.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 929, Year 2022
Publish dateFeb 17, 2022
AuthorsPedro Rebelo-Guiomar / Simone Pellegrino / Kyle C Dent / Aldema Sas-Chen / Leonor Miller-Fleming / Caterina Garone / Lindsey Van Haute / Jack F Rogan / Adam Dinan / Andrew E Firth / Byron Andrews / Alexander J Whitworth / Schraga Schwartz / Alan J Warren / Michal Minczuk /
PubMed AbstractMany cellular processes, including ribosome biogenesis, are regulated through post-transcriptional RNA modifications. Here, a genome-wide analysis of the human mitochondrial transcriptome shows that ...Many cellular processes, including ribosome biogenesis, are regulated through post-transcriptional RNA modifications. Here, a genome-wide analysis of the human mitochondrial transcriptome shows that 2'-O-methylation is limited to residues of the mitoribosomal large subunit (mtLSU) 16S mt-rRNA, introduced by MRM1, MRM2 and MRM3, with the modifications installed by the latter two proteins being interdependent. MRM2 controls mitochondrial respiration by regulating mitoribosome biogenesis. In its absence, mtLSU particles (visualized by cryo-EM at the resolution of 2.6 Å) present disordered RNA domains, partial occupancy of bL36m and bound MALSU1:L0R8F8:mtACP anti-association module, allowing five mtLSU biogenesis intermediates with different intersubunit interface configurations to be placed along the assembly pathway. However, mitoribosome biogenesis does not depend on the methyltransferase activity of MRM2. Disruption of the MRM2 Drosophila melanogaster orthologue leads to mitochondria-related developmental arrest. This work identifies a key checkpoint during mtLSU assembly, essential to maintain mitochondrial homeostasis.
External linksNat Commun / PubMed:35177605 / PubMed Central
MethodsEM (single particle)
Resolution2.89 - 4.19 Å
Structure data

EMDB-13962:
Cryo-EM structure of the human mtLSU assembly intermediate upon MRM2 depletion - class 2
Method: EM (single particle) / Resolution: 3.15 Å

EMDB-13963:
Cryo-EM structure of the human mtLSU assembly intermediate upon MRM2 depletion - class 3
Method: EM (single particle) / Resolution: 2.89 Å

13965

7qh6

EMDB-13965, PDB-7qh6:
Cryo-EM structure of the human mtLSU assembly intermediate upon MRM2 depletion - class 1
Method: EM (single particle) / Resolution: 3.08 Å

EMDB-13966:
Cryo-EM structure of the human mtLSU assembly intermediate upon MRM2 depletion - class 5
Method: EM (single particle) / Resolution: 4.19 Å

13967

7qh7

EMDB-13967, PDB-7qh7:
Cryo-EM structure of the human mtLSU assembly intermediate upon MRM2 depletion - class 4
Method: EM (single particle) / Resolution: 2.89 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • human (human)
KeywordsRIBOSOME / Mitochondria / Assembly / Methyltransferase / MRM2 / RNA modification

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