1. SART3 associates with a post-splicing complex.
- Author
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Klimešová K, Petržílková H, Bařinka C, and Staněk D
- Subjects
- RNA, Small Nuclear genetics, RNA, Small Nuclear metabolism, Ribonucleoprotein, U4-U6 Small Nuclear genetics, Ribonucleoprotein, U4-U6 Small Nuclear metabolism, Ribonucleoprotein, U5 Small Nuclear genetics, Ribonucleoprotein, U5 Small Nuclear metabolism, Ribonucleoprotein, U2 Small Nuclear genetics, Ribonucleoprotein, U2 Small Nuclear metabolism, Ribonucleoproteins, Small Nuclear genetics, Ribonucleoproteins, Small Nuclear metabolism, RNA Splicing genetics, Spliceosomes genetics, Spliceosomes metabolism
- Abstract
SART3 is a multifunctional protein that acts in several steps of gene expression, including assembly and recycling of the spliceosomal U4/U6 small nuclear ribonucleoprotein particle (snRNP). In this work, we provide evidence that SART3 associates via its N-terminal HAT domain with the 12S U2 snRNP. Further analysis showed that SART3 associates with the post-splicing complex containing U2 and U5 snRNP components. In addition, we observed an interaction between SART3 and the RNA helicase DHX15, which disassembles post-splicing complexes. Based on our data, we propose a model that SART3 associates via its N-terminal HAT domain with the post-splicing complex, where it interacts with U6 snRNA to protect it and to initiate U6 snRNA recycling before a next round of splicing., Competing Interests: Competing interests The authors declare no competing or financial interests., (© 2023. Published by The Company of Biologists Ltd.)
- Published
- 2023
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