Journal
NUCLEIC ACIDS RESEARCH
Volume 47, Issue 1, Pages 495-508Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gky1116
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Funding
- Ministry of science and technology of China [2016YFA0500700]
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDPB10, XDB08010101]
- National Natural Science Foundation of China [31330018, 31770805, 91540103]
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Terminal uridylyl transferase (TUTase) is one type of enzyme that modifies RNA molecules by facilitating the post-transcriptional addition of uridyl ribonucleotides to their 3 ends. Recent researches have reported that Drosophila TUTase, Tailor, exhibits an intrinsic preference for RNA substrates ending in 3G, distinguishing it from any other known TUTases. Through this unique feature, Tailor plays a crucial role as the repressor in the biogenesis pathway of splicing-derived mirtron pre-miRNAs. Here we describe crystal structures of core catalytic domain of Tailor and its complexes with RNA stretches 5-AGU-3 and 5-AGUU-3. We demonstrate that R327 and N347 are two key residues contributing cooperatively to Tailor's preference for 3G, and R327 may play an extra role in facilitating the extension of polyuridylation chain. We also demonstrate that conformational stability of the exit of RNA-binding groove also contributes significantly to Tailor's activity. Overall, our work reveals useful insights to explain why Drosophila Tailor can preferentially select RNA substrates ending in 3G and provides important values for further understanding the biological significances of biogenesis pathway of mirtron in flies.
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