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TitleStructural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 5100, Year 2022
Publish dateAug 30, 2022
AuthorsBernhard Kuhle / Marscha Hirschi / Lili K Doerfel / Gabriel C Lander / Paul Schimmel /
PubMed AbstractHuman mitochondrial gene expression relies on the specific recognition and aminoacylation of mitochondrial tRNAs (mtRNAs) by nuclear-encoded mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs). ...Human mitochondrial gene expression relies on the specific recognition and aminoacylation of mitochondrial tRNAs (mtRNAs) by nuclear-encoded mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs). Despite their essential role in cellular energy homeostasis, strong mutation pressure and genetic drift have led to an unparalleled sequence erosion of animal mtRNAs. The structural and functional consequences of this erosion are not understood. Here, we present cryo-EM structures of the human mitochondrial seryl-tRNA synthetase (mSerRS) in complex with mtRNA. These structures reveal a unique mechanism of substrate recognition and aminoacylation. The mtRNA is highly degenerated, having lost the entire D-arm, tertiary core, and stable L-shaped fold that define canonical tRNAs. Instead, mtRNA evolved unique structural innovations, including a radically altered T-arm topology that serves as critical identity determinant in an unusual shape-selective readout mechanism by mSerRS. Our results provide a molecular framework to understand the principles of mito-nuclear co-evolution and specialized mechanisms of tRNA recognition in mammalian mitochondrial gene expression.
External linksNat Commun / PubMed:36042193 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.95 - 4.1 Å
Structure data

26310

7u2a

EMDB-26310, PDB-7u2a:
Cryo-electron microscopy structure of human mt-SerRS in complex with mt-tRNA (GCU)
Method: EM (single particle) / Resolution: 4.1 Å

26311

7u2b

EMDB-26311, PDB-7u2b:
Cryo-electron microscopy structure of human mt-SerRS in complex with mt-tRNA(GCU-TL)
Method: EM (single particle) / Resolution: 4.1 Å

PDB-7tzb:
Crystal structure of the human mitochondrial seryl-tRNA synthetase (mt SerRS) bound with a seryl-adenylate analogue
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

Chemicals

ChemComp-SSA:
5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE

Source
  • homo sapiens (human)
KeywordsLIGASE / Seryl-tRNA synthetase / mitochondria / aminoacylation / translation / tRNA / class II / alpha-beta domain / Ligase/RNA / SerRS / Ligase-RNA complex

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