Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 37, Pages 11541-11546Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1515568112
Keywords
Oskar; structure; RNA-binding; 3 ' UTR; germ cell
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Funding
- Natural Science Foundation of China [31370734, 31430018, 31400670]
- Ministry of Science and Technology of China [2015CB856202]
- National Key New Drug Creation and Manufacturing Program of China [2014ZX09507002]
- Strategic Priority Research Program [XDB08010100]
- Key Research Program of the Chinese Academy of Sciences [KJZDEW-L05]
- Youth Innovation Promotion Association of the Chinese Academy of Sciences
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Oskar (Osk) protein plays critical roles during Drosophila germ cell development, yet its functions in germ-line formation and body patterning remain poorly understood. This situation contrasts sharply with the vast knowledge about the function and mechanism of osk mRNA localization. Osk is predicted to have an N-terminal LOTUS domain (Osk-N), which has been suggested to bind RNA, and a C-terminal hydrolase-like domain (Osk-C) of unknown function. Here, we report the crystal structures of Osk-N and Osk-C. Osk-N shows a homodimer of winged-helix-fold modules, but without detectable RNA-binding activity. Osk-C has a lipase-fold structure but lacks critical catalytic residues at the putative active site. Surprisingly, we found that Osk-C binds the 3'UTRs of osk and nanos mRNA in vitro. Mutational studies identified a region of Osk-C important for mRNA binding. These results suggest possible functions of Osk in the regulation of stability, regulation of translation, and localization of relevant mRNAs through direct interaction with their 3'UTRs, and provide structural insights into a novel protein-RNA interaction motif involving a hydrolase-related domain.
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