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Protein archease (ARCH, ZBTB8OS) is a small, conserved protein that acts as a key cofactor in the tRNA-splicing ligase complex. It facilitates the enzymatic turnover of the catalytic subunit RTCB, specifically promoting the guanylylation of RTCB, a critical step for tRNA ligation. This protein assembles with partners like DDX1, and its interactions are essential for proper tRNA maturation, mRNA splicing, and RNA repair. The structure includes an N-terminal protrusion and a compact C-terminal domain, with intersubunit interactions contributing to protein stability. While not a traditional drug target, its central role in RNA processing and recent links to nervous system injury suggest possible therapeutic relevance[5][1][7][3][9].
No drugs known to target directly. As a cofactor, modulation could theoretically affect tRNA splicing or RNA repair processes.
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