Výsledky vyhledávání - "MESH: Tyrosine-tRNA Ligase"

Computational protein design with a generalized born solvent model: Application to asparaginyl-tRNA synthetase

Autor: Polydorides, Savvas, Amara, Najette, Aubard, C., Plateau, P., Simonson, T., Archontis, Georgios Z.

Publikováno v: Proteins-Structure, Function and Bioinformatics
Proteins-Structure, Function and Bioinformatics, Wiley, 2011, 79 (12), pp.3448-68. ⟨10.1002/prot.23042⟩
Proteins: Structure, Function and Bioinformatics
Proteins Struct.Funct.Bioinformatics

Computational Protein Design (CPD) is a promising method for high throughput protein and ligand mutagenesis. Recently, we developed a CPD method that used a polar-hydrogen energy function for protein interactions and a Coulomb/Accessible Surface Area

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c58df0730662e6ca748e07cda3e3096
https://doi.org/10.1002/prot.23042

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Mutation of the Mitochondrial Tyrosyl-tRNA Synthetase Gene, YARS2, Causes Myopathy, Lactic Acidosis, and Sideroblastic Anemia—MLASA Syndrome

Autor: Peter Hickey, Joëlle Rudinger-Thirion, Richard Giegé, Alison G. Compton, Sandra T. Cooper, Lisa G. Riley, Matthew McKenzie, David R. Thorburn, Michael T. Ryan, Melanie Bahlo, Sze Chern Lim, John Christodoulou

Publikováno v: American Journal of Human Genetics
American Journal of Human Genetics, Elsevier (Cell Press), 2010, 87 (1), pp.52-9. ⟨10.1016/j.ajhg.2010.06.001⟩
The American Journal of Human Genetics

International audience; Mitochondrial respiratory chain disorders are a heterogeneous group of disorders in which the underlying genetic defect is often unknown. We have identified a pathogenic mutation (c.156C>G [p.F52L]) in YARS2, located at chromo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::317a9906f8ed7d1af14a259dea4d7ebb
https://doi.org/10.1016/j.ajhg.2010.06.001

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Virus-Encoded Aminoacyl-tRNA Synthetases: Structural and Functional Characterization of Mimivirus TyrRS and MetRS

Autor: Jean-Michel Claverie, Joëlle Rudinger-Thirion, Chantal Abergel, Richard Giegé

Publikováno v: Journal of Virology
Journal of Virology, 2007, pp.12406-12417
Journal of Virology, 2007, 81 (22), pp.12406-17. ⟨10.1128/JVI.01107-07⟩
Journal of Virology, American Society for Microbiology, 2007, 81 (22), pp.12406-17. ⟨10.1128/JVI.01107-07⟩
Journal of Virology, American Society for Microbiology, 2007, pp.12406-12417
Journal of Virology, American Society for Microbiology, 2007, pp.12406-12417. ⟨10.1128⟩

Aminoacyl-tRNA synthetases are pivotal in determining how the genetic code is translated in amino acids and in providing the substrate for protein synthesis. As such, they fulfill a key role in a process universally conserved in all cellular organism

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e56b242643d733834142c680d7d1c2f3
https://hal.science/hal-00199127

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Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase

Autor: Luc Bonnefond, Magali Frugier, Richard Giegé, Claude Sauter, Joëlle Rudinger-Thirion, Catherine Florentz, Elodie Touzé, Bernard Lorber

Publikováno v: Acta Crystallograph Sect F Struct Biol Cryst Commun
Acta Crystallograph Sect F Struct Biol Cryst Commun, 2007, 63 (Pt 4), pp.338-41. ⟨10.1107/S1744309107012481⟩

International audience; Human mitochondrial tyrosyl-tRNA synthetase and a truncated version with its C-terminal S4-like domain deleted were purified and crystallized. Only the truncated version, which is active in tyrosine activation and Escherichia

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b5ecd17e8583e11f820863055e8159f
https://hal.archives-ouvertes.fr/hal-00167519

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Toward the Full Set of Human Mitochondrial Aminoacyl-tRNA Synthetases: Characterization of AspRS and TyrRS †

Autor: Aurélie Fender, Luc Bonnefond, Richard Giegé, Catherine Florentz, Marie Sissler, Joëlle Rudinger-Thirion

Publikováno v: Biochemistry
Biochemistry, American Chemical Society, 2005, 44 (12), pp.4805-4816. ⟨10.1021/bi047527z⟩

International audience; The human mitochondrion possesses a translational machinery devoted to the synthesis of 13 proteins. While the required tRNAs and rRNAs are produced by transcription of the mitochondrial genome, all other factors needed for pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51ae8f35b1d7766b3143c90c3415636b
https://hal.archives-ouvertes.fr/hal-03365925

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Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces cerevisiae cells

Autor: Julie Soutourina, Pierre Plateau, Sylvain Blanquet

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2000, 275 (42), pp.32535-42. ⟨10.1074/jbc.M005166200⟩

International audience; In Escherichia coli, tyrosyl-tRNA synthetase is known to esterify tRNA(Tyr) with tyrosine. Resulting d-Tyr-tRNA(Tyr) can be hydrolyzed by a d-Tyr-tRNA(Tyr) deacylase. By monitoring E. coli growth in liquid medium, we systemati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::801fdf0d8cc9c8f48efb2cf9014d30fb
https://pubmed.ncbi.nlm.nih.gov/10918062

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D-tyrosyl-tRNA(Tyr) metabolism in Saccharomyces cerevisiae

Autor: Julie Soutourina, Pierre Plateau, Sylvain Blanquet

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2000, 275 (16), pp.11626-30. ⟨10.1074/jbc.275.16.11626⟩

International audience; The Saccharomyces cerevisiae YDL219w (DTD1) gene, which codes for an amino acid sequence sharing 34% identity with the Escherichia coli D-Tyr-tRNA(Tyr) deacylase, was cloned, and its product was functionally characterized. Ove

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::302b3301a79d7584cdf7bc29e11146d4
https://hal-polytechnique.archives-ouvertes.fr/hal-00771806

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Secondary structure of the C-terminal domain of the tyrosyl-transfer RNA synthetase from Bacillus stearothermophilus: a novel type of anticodon binding domain?

Autor: Hugues Bedouelle, Alessandro Pintar, Muriel Delepierre, Valérie Guez, Claire Castagné

Publikováno v: FEBS Letters
FEBS Letters, Wiley, 1999, 446 (1), pp.81-5. ⟨10.1016/S0014-5793(99)00191-X⟩
FEBS Letters, 1999, 446 (1), pp.81-5. ⟨10.1016/S0014-5793(99)00191-X⟩

International audience; The tyrosyl-tRNA synthetase catalyzes the activation of tyrosine and its coupling to the cognate tRNA. The enzyme is made of two domains: an N-terminal catalytic domain and a C-terminal domain that is necessary for tRNA bindin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29bbe1e99d5045eda743595ff8352166
https://hal-pasteur.archives-ouvertes.fr/pasteur-00370448

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