SART3 associates with a post-splicing complex

0570767 - ÚMG 2024 RIV GB eng J - Journal Article
Klimešová, Klára - Petržílková, Hana - Bařinka, Cyril - Staněk, David
SART3 associates with a post-splicing complex.
Journal of Cell Science. Roč. 136, č. 2 (2023), č. článku jcs260380. ISSN 0021-9533. E-ISSN 1477-9137
R&D Projects: GA ČR GA21-04132S
Institutional support: RVO:68378050 ; RVO:86652036
Keywords : Splicing * Recycling * U6 snRNA * U2 snRNP
OECD category: Cell biology
Impact factor: 4, year: 2022
Method of publishing: Limited access
https://journals.biologists.com/jcs/article-abstract/136/2/jcs260380/286729/SART3-associates-with-a-post-splicing-complex?redirectedFrom=fulltext

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.
Permanent Link: https://hdl.handle.net/11104/0342107