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• W2014560215 abstract "Selenocysteinyl-tRNA(Sec), cysteinyl-tRNA(Cys), glutaminyl-tRNA(Gln), and asparaginyl-tRNA(Asn) in many organisms are formed in an indirect pathway in which a non-cognate amino acid is first attached to the tRNA. This non-cognate amino acid is then converted to the cognate amino acid by a tRNA-dependent modifying enzyme. The in vitro characterization of these modifying enzymes is challenging due to the fact the substrate, aminoacyl-tRNA, is labile and requires a prior enzymatic step to be synthesized. The need to separate product aa-tRNA from unreacted substrate is typically a labor- and time-intensive task; this adds another impediment in the investigation of these enzymes. Here, we review four different approaches for studying these tRNA-dependent amino acid modifications. In addition, we describe in detail a [32P]/nuclease P1 assay for glutaminyl-tRNA(Gln) and asparaginyl-tRNA(Asn) formation which is sensitive, enables monitoring of the aminoacyl state of the tRNA, and is less time consuming than some of the other techniques. This [32P]/nuclease P1 method should be adaptable to studying tRNA-dependent selenocysteine and cysteine synthesis." @default.
• W2014560215 created "2016-06-24" @default.
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• W2014560215 date "2008-02-01" @default.
• W2014560215 modified "2023-10-13" @default.
• W2014560215 title "Assays for transfer RNA-dependent amino acid biosynthesis" @default.
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• W2014560215 doi "https://doi.org/10.1016/j.ymeth.2007.06.010" @default.
• W2014560215 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2266967" @default.
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