SART3 associates with a post-splicing complex

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F23%3A00570767" target="_blank" >RIV/68378050:_____/23:00570767 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/86652036:_____/23:00570767

Výsledek na webu

<a href="https://journals.biologists.com/jcs/article-abstract/136/2/jcs260380/286729/SART3-associates-with-a-post-splicing-complex?redirectedFrom=fulltext" target="_blank" >https://journals.biologists.com/jcs/article-abstract/136/2/jcs260380/286729/SART3-associates-with-a-post-splicing-complex?redirectedFrom=fulltext</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1242/jcs.260380" target="_blank" >10.1242/jcs.260380</a>

Jazyk výsledku

angličtina

Název v původním jazyce

SART3 associates with a post-splicing complex

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

SART3 associates with a post-splicing complex

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10601 - Cell biology

Projekt

<a href="/cs/project/GA21-04132S" target="_blank" >GA21-04132S: Molekulární mechanismus tvorby spliceosomálního snRNP částic</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Cell Science

ISSN

0021-9533

e-ISSN

1477-9137

Svazek periodika

136

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

jcs260380

Kód UT WoS článku

000932291900003

EID výsledku v databázi Scopus

2-s2.0-85147046154