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Cytosolic thiouridylase subunit 1 (CTU1) is a conserved enzyme that, together with CTU2, forms the cytosolic tRNA 2-thiolation complex. CTU1 catalyzes the 2-thiolation at the 34th (wobble) uridine position of the anticodon loop in specific cytoplasmic tRNAs (notably tRNA^Lys^, tRNA^Glu^, and tRNA^Gln^) as part of the mcm^5^s^2^U^34^ modification. This post-transcriptional tRNA modification is critical for proper codon-anticodon recognition, translation fidelity, and global protein synthesis. Loss or deficiency of CTU1 disrupts these processes and results in genome instability, errors in translation, cell cycle arrest, impaired cell proliferation, defective angiogenesis, and abnormal nervous and erythrocyte development. Human gene mutations or dysfunction of CTU1 have been linked to multiple disease states, including congenital heart defects, developmental delay, and cancer, suggesting important roles in both normal physiology and disease. CTU1 is not currently a known drug target, and there are no drugs or biomarkers specifically associated with its modulation[1][2][3][5].
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