期刊
STRUCTURE
卷 30, 期 7, 页码 983-+出版社
CELL PRESS
DOI: 10.1016/j.str.2022.04.002
关键词
-
资金
- NIH [R01 GM124622, GM138838, S10 RR025080, U24 GM116788, S10 RR024564]
- Florida State University
- DOE Office of Biological and Environmental Research [KP160711]
This study characterized the structures and conformations of modified and pseudouridine-free ribosomes using electron cryomicroscopy. It found that pseudouridine stabilizes key functional motifs by establishing water-mediated close contacts with the phosphate backbone, while the absence of pseudouridine leads to abnormal inter-subunit movements.
Pseudouridine, the most abundant form of RNA modification, is known to play important roles in ribosome function. Mutations in human DKC1, the pseudouridine synthase responsible for catalyzing the ribosome RNA modification, cause translation deficiencies and are associated with a complex cancer predisposition. The structural basis for how pseudouridine impacts ribosome function remains uncharacterized. Here, we characterized structures and conformations of a fully modified and a pseudouridine-free ribosome from Saccharomyces cerevisiae in the absence of ligands or when bound with translocation inhibitor cyclohexi-mide by electron cryomicroscopy. In the modified ribosome, the rearranged N1 atom of pseudouridine is observed to stabilize key functional motifs by establishing predominately water-mediated close contacts with the phosphate backbone. The pseudouridine-free ribosome, however, is devoid of such interactions and displays conformations reflective of abnormal inter-subunit movements. The erroneous motions of the pseudouridine-free ribosome may explain its observed deficiencies in translation.
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