Publications by authors named "Adeline Pichard-Kostuch"
TsaC/Sua5 family of enzymes catalyzes the first step in the synthesis of N6-threonyl-carbamoyl adenosine (tA) one of few truly ubiquitous tRNA modifications important for translation accuracy. TsaC is a single domain protein while Sua5 proteins contains a TsaC-like domain and an additional SUA5 domain of unknown function. The emergence of these two proteins and their respective mechanisms for tA synthesis remain poorly understood.
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- Researchers have developed a method for single-molecule protein sequencing that accurately identifies peptide sequences in real time.
- This technique uses dye-labeled amino acid recognizers and aminopeptidases to probe single peptides while recording fluorescence data on a semiconductor chip.
- The method shows potential for detailed analysis of proteins, including the ability to detect single amino acid changes and modifications, paving the way for more accessible proteomic research.
-threonyl-carbamoyl adenosine (tA) is a universal tRNA modification found at position 37, next to the anticodon, in almost all tRNAs decoding ANN codons (where N = A, U, G, or C). tA stabilizes the codon-anticodon interaction and hence promotes translation fidelity. The first step of the biosynthesis of tA, the production of threonyl-carbamoyl adenylate (TC-AMP), is catalyzed by the Sua5/TsaC family of enzymes.
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