This domain is found at the C-terminal in human ATP-dependent RNA helicase DHX37 and related proteins. DHX37 is a component of the human SSU processome and plays an important role in processome maturation. This domain folds into an array of ��-helices and it is involved in protein-protein interactions with other components such as PWP2 and WDR36 [, ]. It is also involved in the recruitment of DHX37 to the processome [].
This family of proteins is involved in the early stages of ribosome biogenesis, specifically in the assembly of the small subunit (SSU) processome. These proteins are found in the nucleolus and are associated with the nascent pre-ribosomal RNA. They collaborate with ribosome biogenesis factors, an RNA chaperone, and ribosomal proteins to facilitate RNA folding, chemical modifications, structural rearrangements, and cleavage. Additionally, they contribute to the targeted degradation of pre-ribosomal RNA by the RNA exosome. A key regulatory function of these proteins is to prevent the premature recruitment of the helicase DHX37 during the pre-ribosomal RNA processing stages.
