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NOP protein chaperone 1 is an intrinsically disordered protein that serves as a client-loading cofactor for the PAQosome (HSP90/R2TP complex and prefoldin-like module) to facilitate the assembly of box C/D small nucleolar ribonucleoproteins. It acts specifically by bridging NOP58 and the RUVBL1/2 AAA+ ATPase complex, ensuring selective incorporation of NOP58 and proper snoRNP biogenesis. NOPCHAP1 shows robust binding to both yeast and human NOP58 proteins but minimal interaction with homologous proteins NOP56 and PRPF31. This selectivity supports proper ribonucleoprotein complex formation in the nucleus. Knockout studies indicate NOPCHAP1 is dispensable for cell growth and cell cycle progression but is important for maintaining NOP58 protein levels and assembly during early steps in snoRNP biogenesis.
Not applicable (No direct drug mechanisms described for this protein)
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