RNA pseudouridine synthase D4 (RPUSD4)

RNA pseudouridine synthase D4 (RPUSD4) is a mitochondrial enzyme that catalyzes the isomerization of uridine to pseudouridine in mitochondrial 16S rRNA and mitochondrial tRNA^Phe^, with essential roles in mitochondrial ribosome assembly, stability of 16S mt-rRNA, and overall mitochondrial translation. The protein is nuclear-encoded but localizes to the mitochondrial matrix and nucleoplasm, functioning in mitochondrial RNA granules as part of a protein module with other RNA-modifying proteins. RPUSD4 is required for the proper assembly of the mitochondrial ribosomal large subunit and is also implicated in the pseudouridylation of pre-mRNA in the nucleus, affecting RNA splicing. Loss of RPUSD4 leads to mitochondrial translation impairment, OXPHOS (oxidative phosphorylation) deficiency, and is essential for cell viability, underlying its involvement in mitochondrial disease phenotypes connected to defects in energy metabolism[1][2][3][4]. Summary of key actions: - Catalyzes specific pseudouridylation of uridine residues in mitochondrial rRNAs and tRNAs[1][2][3]. - Required for assembly and function of mitochondrial ribosomes, and hence efficient mitochondrial protein synthesis[2][3][4]. - Loss leads to instability of 16S mt-rRNA and severe defects in mitochondrial translation and respiration, ultimately resulting in cell death[2][3]. - Identified as an essential gene in human cells and a component of a mitochondrial RNA granule functional module[3][4]. - No known direct pharmacological modulators or drugs target RPUSD4 as of the current literature[1][2][3][4].

Other names

Pseudouridylate synthase RPUSD4, mitochondrialFLJ14494RNA pseudouridylate synthase domain-containing protein 4RNA pseudouridylate synthase domain containing 4mitochondrial RNA pseudouridine synthase RPUSD4

Mechanism for hypothetical targeting would likely involve inhibition or modulation of RNA pseudouridylation.