| |  Online-Ressource |
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| Verfasst von: | Ahmed, Nabeel [VerfasserIn]  |
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| | Friedrich, Ulrike A. [VerfasserIn] |
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| | Sormanni, Pietro [VerfasserIn] |
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| | Ciryam, Prajwal [VerfasserIn] |
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| | Altman, Naomi S. [VerfasserIn] |
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| | Bukau, Bernd [VerfasserIn] |
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| | Kramer, Günter [VerfasserIn] |
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| | O'Brien, Edward P. [VerfasserIn] |
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| Titel: | Pairs of amino acids at the P- and A-sites of the ribosome predictably and causally modulate translation-elongation rates |
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| Verf.angabe: | Nabeel Ahmed, Ulrike A. Friedrich, Pietro Sormanni, Prajwal Ciryam, Naomi S. Altman, Bernd Bukau, Günter Kramer and Edward P. O'Brien |
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| E-Jahr: | 2020 |
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| Jahr: | 3 November 2020 |
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| Umfang: | 15 S. |
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| Teil: | volume:432 |
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| | year:2020 |
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| | number:24 |
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| | pages:1-15 |
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| | extent:15 |
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| Fussnoten: | Gesehen am 19.02.2021 |
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| Titel Quelle: | Enthalten in: Journal of molecular biology |
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| Ort Quelle: | Amsterdam [u.a.] : Elsevier, 1959 |
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| Jahr Quelle: | 2020 |
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| Band/Heft Quelle: | 432(2020,24) Artikel-Nummer 166696, 15 Seiten |
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| ISSN Quelle: | 1089-8638 |
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| Abstract: | Variation in translation-elongation kinetics along a transcript’s coding sequence plays an important role in the maintenance of cellular protein homeostasis by regulating co-translational protein folding, localization, and maturation. Translation-elongation speed is influenced by molecular factors within mRNA and protein sequences. For example, the presence of proline in the ribosome’s P- or A-site slows down translation, but the effect of other pairs of amino acids, in the context of all 400 possible pairs, has not been characterized. Here, we study Saccharomyces cerevisiae using a combination of bioinformatics, mutational experiments, and evolutionary analyses, and show that many different pairs of amino acids and their associated tRNA molecules predictably and causally encode translation rate information when these pairs are present in the A- and P-sites of the ribosome independent of other factors known to influence translation speed including mRNA structure, wobble base pairing, tripeptide motifs, positively charged upstream nascent chain residues, and cognate tRNA concentration. The fast-translating pairs of amino acids that we identify are enriched four-fold relative to the slow-translating pairs across Saccharomyces cerevisiae’s proteome, while the slow-translating pairs are enriched downstream of domain boundaries. Thus, the chemical identity of amino acid pairs contributes to variability in translation rates, elongation kinetics are causally encoded in the primary structure of proteins, and signatures of evolutionary selection indicate their potential role in co-translational processes. |
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| DOI: | doi:10.1016/j.jmb.2020.10.030 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1016/j.jmb.2020.10.030 |
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| | Volltext: https://www.sciencedirect.com/science/article/pii/S0022283620306148 |
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| | DOI: https://doi.org/10.1016/j.jmb.2020.10.030 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | amino acid pairs |
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| | elongation rates |
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| | ribosome profiling |
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| | translation |
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| K10plus-PPN: | 1748712861 |
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| Verknüpfungen: | → Zeitschrift |
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Pairs of amino acids at the P- and A-sites of the ribosome predictably and causally modulate translation-elongation rates / Ahmed, Nabeel [VerfasserIn]; 3 November 2020 (Online-Ressource)
