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TitleCiliate mitoribosome illuminates evolutionary steps of mitochondrial translation.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateJun 18, 2020
AuthorsVictor Tobiasson / Alexey Amunts /
PubMed AbstractTo understand the steps involved in the evolution of translation, we used , a ciliate with high coding capacity of the mitochondrial genome, as the model organism and characterized its mitochondrial ...To understand the steps involved in the evolution of translation, we used , a ciliate with high coding capacity of the mitochondrial genome, as the model organism and characterized its mitochondrial ribosome (mitoribosome) using cryo-EM. The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit, while the large subunit lacks 5S rRNA. The structure also shows that the small subunit head is constrained, tRNA binding sites are formed by mitochondria-specific protein elements, conserved protein bS1 is excluded, and bacterial RNA polymerase binding site is blocked. We provide evidence for anintrinsic protein targeting system through visualization of mitochondria-specific mL105 by the exit tunnel that would facilitate the recruitment of a nascent polypeptide. Functional protein uS3m is encoded by three complementary genes from the nucleus and mitochondrion, establishing a link between genetic drift and mitochondrial translation. Finally, we reannotated nine open reading frames in the mitochondrial genome that code for mitoribosomal proteins.
External linksElife / PubMed:32553108 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.7 Å
Structure data

EMDB-11032: The mitochondrial ribosome from Tetrahymena thermophila
PDB-6z1p: Structure of the mitochondrial ribosome from Tetrahymena thermophila
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-11033:
The mitochondrial ribosome from Tetrahymena thermophila, large subunit mask
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-11034:
The mitochondrial ribosome from Tetrahymena thermophila, small subunit mask
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-11035:
The mitochondrial ribosome from Tetrahymena thermophila, central protuberance mask
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-11036:
The mitochondrial ribosome from Tetrahymena thermophila, L7/L12 stalk mask
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-11037:
The mitochondrial ribosome from Tetrahymena thermophila, small subunit head mask
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-11038:
The mitochondrial ribosome from Tetrahymena thermophila, small subunit back protuberance mask
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

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

Source
  • Tetrahymena thermophila SB210 (eukaryote)
  • tetrahymena thermophila (strain sb210) (eukaryote)
KeywordsRIBOSOME / Mitochondrial ribosome / mitochondria / ciliate / tetrahymena

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