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Cytoplasmic tRNA 2-thiolation protein 2 (CTU2) is a highly conserved protein that forms a complex with CTU1 (known as Ctu1–Ctu2 or cytosolic thiouridylase) responsible for the 2-thiolation of uridine at the wobble position (U34) of several cytosolic tRNAs, specifically those for lysine, glutamine, and glutamate[1][2][3][4]. This modification, mcm^5^S^2^U, is crucial for maintaining the fidelity and efficiency of translation by restricting aberrant base pairing and reducing frameshifting—ultimately supporting accurate decoding of mRNA by the ribosome[1][2][3]. Loss of function or inactivation of the CTU1–CTU2 complex leads to unthiolated tRNAs, associated with genome instability, defective cell growth, and impaired viability under stress, but there is no direct implication as a receptor, transporter, or canonical therapeutic target[1][3][4]. CTU2 does not have known direct disease associations, approved drugs, or biomarker use cases, but it is essential for the proper translation machinery and genomic integrity in eukaryotic cells[1][2][4].
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