SART3 associates with a post-splicing complex
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
Grant support
21-04132S
Grantova Agentura ɨeska Republiky
RVO86652036
Akademie Vʃd ɨeska Republiky
21-04132S
Grantová Agentura České Republiky
RVO68378050
Ústav Molekulární Genetiky, Akademie Věd České Republiky
RVO86652036
Akademie Věd České Republiky
PubMed
36620952
DOI
10.1242/jcs.260380
PII: 286729
Knihovny.cz E-resources
- Keywords
- Recycling, Splicing, U2 snRNP, U6 snRNA,
- MeSH
- Ribonucleoprotein, U2 Small Nuclear genetics metabolism MeSH
- Ribonucleoprotein, U4-U6 Small Nuclear genetics metabolism MeSH
- Ribonucleoprotein, U5 Small Nuclear genetics metabolism MeSH
- Ribonucleoproteins, Small Nuclear genetics metabolism MeSH
- RNA, Small Nuclear genetics metabolism MeSH
- RNA Splicing * genetics MeSH
- Spliceosomes * genetics metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Ribonucleoprotein, U2 Small Nuclear MeSH
- Ribonucleoprotein, U4-U6 Small Nuclear MeSH
- Ribonucleoprotein, U5 Small Nuclear MeSH
- Ribonucleoproteins, Small Nuclear MeSH
- RNA, Small Nuclear MeSH
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.
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