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ATP-dependent RNA helicase DDX55 is a nucleoplasmic enzyme that catalyzes the unwinding and remodeling of RNA structures by hydrolyzing ATP, primarily participating in the maturation of large ribosomal subunit pre-rRNAs[1][3]. It localizes to the nucleoplasm and associates specifically with pre-ribosomal complexes, functioning as a ribosome biogenesis factor and contributing to proper assembly and processing of the ribosome's large subunit. DDX55 selectively binds double-stranded RNA, with its C-terminal domain required for nuclear import and pre-ribosome substrate specificity[1]. It contains a nuclear localization signal in the C-terminal region and is evolutionarily conserved with related helicases in yeast and other species. No drugs, known disease-causing mutations, or biomarker roles are currently reported for DDX55[1][3].
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