| Description |
1 online resource (xiii, 423 pages) : illustrations (chiefly color) |
| Series |
The enzymes ; 48 |
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Enzymes ; v. 48
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| Contents |
Intro -- Biology of Aminoacyl-tRNA Synthetases -- Copyright -- Contents -- Contributors -- Preface -- Chapter One: The endless frontier of tRNA synthetases -- 1. aaRSs establish the genetic code -- 2. Problems when simplicity is not quite enough -- 3. Orthogonal functions created from pieces and decorations -- 4. Functions and diseases linked to tRNA synthetases -- 5. Therapeutics with splice variants -- 6. The endless frontier -- Acknowledgements -- Chapter Two: The evolution of aminoacyl-tRNA synthetases: From dawn to LUCA -- 1. Introduction -- 2. The aaRS conundrum |
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2.1. Bacterial PheRS post-transfer editing machinery primarily prevents m-Tyr misincorporation -- 2.2. Eukaryotic PheRS post-transfer editing machinery primarily targets p-Tyr-tRNA -- 3. AlaRS editing domain and trans-editing factors ubiquitously prevent Ser and Gly misincorporation -- 3.1. AlaRS editing domain deacylates Ser- and Gly-tRNA -- 3.2. AlaXps are autonomous AlaRS editing domain homologs -- 3.2.1. AlaX-S is likely the predecessor of AlaRS and ThrRS editing domains -- 3.2.2. Mammalian AlaX-M trans-editing of Ser- and Gly-tRNA |
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2.4. Acid-base chemistry vs substrate-assisted catalysis in tRNA aminoacylation -- 3. Metals in AARS-mediated catalysis -- 3.1. Divalent metal cofactors facilitate amino acid activation -- 3.2. CysRS and ThrRS each use an active site Zn cofactor for amino acid discrimination and catalysis -- 3.3. Other examples of metal participation in AARS function -- 4. Conclusion -- References -- Chapter Four: Trans-editing by aminoacyl-tRNA synthetase-like editing domains -- 1. Introduction -- 2. Proofreading by PheRS editing domain prevents m-Tyr and p-Tyr misincorporation |
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3. A temporal perspective for aaRS evolution -- 3.1. Prebiotic biochemical period -- 3.2. Prebiotic macromolecular period -- 3.3. Pre-LUCA biological period -- 3.4. Post-LUCA period -- 4. Summary -- Acknowledgments -- References -- Chapter Three: Putting amino acids onto tRNAs: The aminoacyl-tRNA synthetases as catalysts -- 1. Introduction -- 1.1. The reactions catalyzed by the AARSs -- 1.2. Class-defining features of AARSs -- 2. Mechanistic strategies used by the AARSs -- 2.1. Rate-limiting step of aminoacylation -- 2.2. Protein dynamics and induced fit -- 2.3. Transition state stabilization |
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3.3. d-aminoacyl-tRNA deacylases prevent Gly misincorporation -- 3.4. Animal-specific DTD edits Ala-tRNA (G4:U69) error unique to eukaryotes -- 4. Functional convergence of distinct ThrRS editing domains prevent Ser and Ala misincorporation -- 4.1. Oxidative stress regulates N2 domain hydrolysis of mischarged Ser-tRNA -- 4.1.1. Zinc availability regulates trans-editing by ThrRS isoforms in cyanobacteria -- 4.2. Post-transfer editing by eukaryotic ThrRS isoforms TARS, TARS2, and TARSL2 -- 4.3. Post-transfer editing by archaeal ThrRS is mediated by a DTD-like editing domain |
| Summary |
Biology of Aminoacyl-tRNA Synthetases, Volume 48 in The Enzymes series, highlights new advances in the field, with this new volume presenting interesting chapters on A narrative about our work on the endless frontier of editing, The puzzling evolution of aminoacyl-tRNA synthetases, Structural basis of the tRNA recognition by aminoacyl-tRNA synthetases, Catalytic strategies of aminoacyl-tRNA synthetases, Trans-editing by aminoacyl-tRNA synthetase-like editing domains, Adaptive and maladaptive mistranslation arising from aminoacyl-tRNA synthetases, Non-canonical inputs and outputs of tRNA aminoacylation, Structure and function of multi-tRNA synthetase complexes, Mitochondrial aminoacyl-tRNA synthetases, Non-canonical functions of human cytoplasmic tyrosyl-, tryptophanyl- and other aminoacyl-tRNA synthetases, and much more |
| Subject |
Aminoacyl-tRNA synthetases.
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Amino Acyl-tRNA Synthetases
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Aminoacyl-tRNA synthetases.
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| Genre/Form |
Electronic books.
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| Form |
Electronic book
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| Author |
Kaguni, Laurie, editor.
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Ribas de Pouplana, Lluís. editor.
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| ISBN |
0128202610 |
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9780128202616 |
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