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Biology of aminoacyl-tRNA synthetases/
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...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | , |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Cambridge, MA :
Academic Press,
2020.
|
| Edición: | First edition. |
| Colección: | Enzymes ;
v. 48. |
| Temas: | |
| Acceso en línea: | Texto completo |
MARC
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| 019 | |a 1202229409 | ||
| 020 | |a 9780128202616 |q (electronic bk.) | ||
| 020 | |a 0128202610 |q (electronic bk.) | ||
| 020 | |z 9780128202609 | ||
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| 035 | |a (OCoLC)1202058854 |z (OCoLC)1202229409 | ||
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| 082 | 0 | 4 | |a 572/.79 |2 23 |
| 245 | 0 | 0 | |a Biology of aminoacyl-tRNA synthetases/ |c edited by Llu�is Ribas de Pouplana, Laurie S. Kaguni |
| 250 | |a First edition. | ||
| 260 | |a Cambridge, MA : |b Academic Press, |c 2020. | ||
| 300 | |a 1 online resource (xiii, 423 pages) : |b illustrations (chiefly color) | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
| 490 | 1 | |a The enzymes ; |v 48 | |
| 505 | 2 | |a 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 | |
| 505 | 8 | |a 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 | |
| 505 | 8 | |a 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 | |
| 505 | 8 | |a 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 | |
| 505 | 8 | |a 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 | |
| 520 | |a 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. | ||
| 650 | 0 | |a Aminoacyl-tRNA synthetases. | |
| 650 | 2 | |a Amino Acyl-tRNA Synthetases |0 (DNLM)D000604 | |
| 650 | 6 | |a Aminoacyl-ARNt synth�etases. |0 (CaQQLa)201-0333988 | |
| 650 | 7 | |a Aminoacyl-tRNA synthetases. |2 fast |0 (OCoLC)fst00807653 | |
| 700 | 1 | |a Ribas de Pouplana, Llu�is. |e editor. |4 edt | |
| 700 | 1 | |a Kaguni, Laurie, |e editor |4 edt | |
| 776 | 0 | 8 | |i Print version: |z 9780128202616 |
| 776 | 0 | 8 | |i Print version: |z 0128202602 |z 9780128202609 |w (OCoLC)1150943590 |
| 830 | 0 | |a Enzymes ; |v v. 48. | |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/18746047/48 |z Texto completo |