The human pseudouridine synthase PUS7 recognizes RNA with an extended multi-domain binding surface.

ABSTRACT: The human pseudouridine synthase PUS7 is a versatile RNA modification enzyme targeting many RNAs thereby playing a critical role in development and brain function. Whereas all target RNAs of PUS7 share a consensus sequence, additional recognition elements are likely required, and the structural basis for RNA binding by PUS7 is unknown. Here, we characterize the structure-function relationship of human PUS7 reporting its X-ray crystal structure at 2.26 Å resolution. Compared to its bacterial homolog, human PUS7 possesses two additional subdomains, and structural modeling studies suggest that these subdomains contribute to tRNA recognition through increased interactions along the tRNA substrate. Consistent with our modeling, we find that all structural elements of tRNA are required for produ

SUBMITTER: Guegueniat J 

PROVIDER: S-EPMC8599909 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature