Pseudouridine synthase 3 (PUS3)

**Pseudouridine synthase 3 (PUS3)** is a stand-alone RNA-modifying enzyme that catalyzes the site-specific isomerization of uridine to pseudouridine in various RNA molecules, particularly in cytoplasmic and mitochondrial tRNAs at positions 38/39 of the anticodon loop[1]. PUS3 also acts on certain mRNAs and long non-coding RNAs, contributing to the regulation of gene expression. The enzyme ensures proper RNA folding and translation efficiency, and its loss results in growth defects in yeast and significant neurodevelopmental disorders in humans[1]. As a member of the broader pseudouridine synthase family, PUS3 contains a conserved catalytic domain with a key aspartate residue mediating the ribose deprotonation and uracil ring isomerization required for pseudouridine formation[1][3]. The enzyme's activity is essential for the structural stability and function of multiple classes of RNA, and broader defects in pseudouridylation have been associated with diverse human diseases, including neurodevelopmental disorders and potentially cancer through misregulation of RNA processing[1][2]. **Notes:** - Pseudouridine synthase 3 is not a receptor, but an enzyme. - No known drugs directly target PUS3 as of current data; research is ongoing into the roles of pseudouridine synthases in disease and potential therapeutic targeting[2]. - The information above is consistent with current scientific consensus and nomenclature.

Other names

Deg1PUS3Depressed growth rate protein

Enzymatic isomerization of uridine to pseudouridine in RNA