Spectrophotometric assays for monitoring tRNA aminoacylation and aminoacyl-tRNA hydrolysis reactions

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• 作者：Eric A. First ; ^{efirst@lsuhsc.edu} ; Charles J. Richardson¹
• 关键词：A340 ; absorbance at 340  ; nm ; AMP ; adenosine 5&prime ; -monophosphate ; IMP ; inosine 5&prime ; -monophosphate ; XMP ; xanthine 5&prime ; -monophosphate ; PPi ; inorganic pyrophosphate ; l-Tyr ; d-Tyr ; l- and d-tyrosine ; NAD+ ; NADH ; oxidized and reduced nicotine adenine dinucleotide ; MESG ; 2-amino-6-mercapto-7-methyl purine ribonucleoside ; aaRS ; aminoacyl-tRNA synthetase ; TyrRS ; tyrosyl-tRNA synthetase ; TyrRS-FRSed ; chimeric protein consisting of the editing domain from Pyrococcus horikoshii phenylalanyl-t
• 刊名：Methods
• 出版年：2017
• 出版时间：15 January 2017
• 年：2017
• 卷：113
• 期：Complete
• 页码：3-12
• 全文大小：1736 K
• 卷排序：113

文摘

Spectrophotometric assay to monitor tyrosyl-tRNA synthetase activity. Recycling the tRNA substrate in aminoacyl-tRNA synthetase assays. Adaptation of the tyrosyl-tRNA synthetase assay to monitor cyclodipeptide synthase, d-tyrosyl-tRNA deacylase, and post-transfer editing activity. Adaptation of the tyrosyl-tRNA synthetase assay to monitor the activity of other aminoacyl-tRNA synthetases.