Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA

Mitochondrial tRNAs are indispensable and yet underwent an extreme mutational erosion. The authors report the structures of a mitochondrial aaRS-tRNA complex and show how the most degenerated of all human mtRNAs is recognized by its cognate synthetase to maintain mitochondrial gene expression.

Bibliographic Details
Main Authors: Bernhard Kuhle, Marscha Hirschi, Lili K. Doerfel, Gabriel C. Lander, Paul Schimmel
Format: Article
Language:English
Published: Nature Portfolio 2022-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-32544-1
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author Bernhard Kuhle
Marscha Hirschi
Lili K. Doerfel
Gabriel C. Lander
Paul Schimmel
author_facet Bernhard Kuhle
Marscha Hirschi
Lili K. Doerfel
Gabriel C. Lander
Paul Schimmel
author_sort Bernhard Kuhle
collection DOAJ
description Mitochondrial tRNAs are indispensable and yet underwent an extreme mutational erosion. The authors report the structures of a mitochondrial aaRS-tRNA complex and show how the most degenerated of all human mtRNAs is recognized by its cognate synthetase to maintain mitochondrial gene expression.
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spelling doaj.art-c61de2c5906644379fa90b8007176bd02022-12-22T03:12:23ZengNature PortfolioNature Communications2041-17232022-08-0113111210.1038/s41467-022-32544-1Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNABernhard Kuhle0Marscha Hirschi1Lili K. Doerfel2Gabriel C. Lander3Paul Schimmel4Department of Molecular Medicine, The Scripps Research InstituteDepartment of Integrative Structural and Computational Biology, The Scripps Research InstituteDepartment of Integrative Structural and Computational Biology, The Scripps Research InstituteDepartment of Integrative Structural and Computational Biology, The Scripps Research InstituteDepartment of Molecular Medicine, The Scripps Research InstituteMitochondrial tRNAs are indispensable and yet underwent an extreme mutational erosion. The authors report the structures of a mitochondrial aaRS-tRNA complex and show how the most degenerated of all human mtRNAs is recognized by its cognate synthetase to maintain mitochondrial gene expression.https://doi.org/10.1038/s41467-022-32544-1
spellingShingle Bernhard Kuhle
Marscha Hirschi
Lili K. Doerfel
Gabriel C. Lander
Paul Schimmel
Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA
Nature Communications
title Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA
title_full Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA
title_fullStr Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA
title_full_unstemmed Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA
title_short Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA
title_sort structural basis for shape selective recognition and aminoacylation of a d armless human mitochondrial trna
url https://doi.org/10.1038/s41467-022-32544-1
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