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La tyrosyl-ARNt synthétase mitochondriale humaine : originalités fonctionnelles, structurales et place dans l'évolution

Abstract : My thesis focuses on the functional and structural characterization of the tyrosine specific aminoacylation system from human mitochondria. Unlike the general situation found in other aminoacylation systems, cross-reactions between bacteria and archea/eukarya are impossible due to the difference of tRNATyr first base pair. Human mitochondrial tyrosyl-tRNA synthetase (TyrRS) is the first known TyrRS overcoming the species barrier and that doesn't discriminate tRNATyr for their first base pair. The mitochondrial TyrRS is an homodimer of elongated shape that will like likely bind one tRNATyr molecule across both subunits. It differs from other TyrRS by the presence of two insertions at its surface, the first one being potentially implicated in the tRNATyr binding and the second one that could serve as a co-factor binding interface.
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https://tel.archives-ouvertes.fr/tel-00196315
Contributor : Isabelle Martin <>
Submitted on : Wednesday, December 12, 2007 - 2:57:15 PM
Last modification on : Thursday, April 23, 2020 - 2:26:32 PM
Long-term archiving on: : Monday, April 12, 2010 - 7:10:14 AM

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  • HAL Id : tel-00196315, version 1

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Luc Bonnefond. La tyrosyl-ARNt synthétase mitochondriale humaine : originalités fonctionnelles, structurales et place dans l'évolution. Biochimie [q-bio.BM]. Université Louis Pasteur - Strasbourg I, 2007. Français. ⟨tel-00196315⟩

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