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  Amino acid modifications on tRNA

Yuan, J., Sheppard, K., & Soll, D. (2008). Amino acid modifications on tRNA. ACTA BIOCHIMICA ET BIOPHYSICA SINICA, 40(7), 539-553. doi:10.1111/j.1745-7270.2008.00435.x.

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Yuan, Jing1, Autor                 
Sheppard, Kelly2, Autor
Soll, Dieter2, Autor
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1Department of Molecular Biophysics and Biochemistry, Yale University, USA, ou_persistent22              
2external, ou_persistent22              

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 Zusammenfassung: The accurate formation of cognate aminoacyl-transfer RNAs (aa-tRNAs) is essential for the fidelity of translation. Most amino acids are esterified onto their cognate tRNA isoacceptors directly by aa-tRNA synthetases. However, in the case of four amino acids (Gln, Asn, Cys and Sec), aminoacyl-tRNAs are made through indirect pathways in many organisms across all three domains of life. The process begins with the charging of noncognate amino acids to tRNAs by a specialized synthetase in the case of Cys-tRNA(Cys) formation or by synthetases with relaxed specificity, such as the non-di scr iminating glutamyl-tRNA, non-disc rimi nati ng aspartyl-tRNA and seryl-tRNA synthetases. The resulting misacylated tRNAs are then converted to cognate pairs through transformation of the amino acids on the tRNA, which is catalyzed by a group of tRNA-dependent modifying enzymes, such as tRNA-dependent amidotransferases, Sep-tRNA:Cys-tRNA synthase, O-phosphoseryl-tRNA kinase and Sep-tRNA:Sec-tRNA synthase. The majority of these indirect pathways are widely spread in all domains of life and thought to be part of the evolutionary process.

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 Datum: 2008
 Publikationsstatus: Erschienen
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Titel: ACTA BIOCHIMICA ET BIOPHYSICA SINICA
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 40 (7) Artikelnummer: - Start- / Endseite: 539 - 553 Identifikator: ISSN: 1672-9145