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SART3 associates with a post-splicing complex

The result's identifiers

  • Result code in 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>

  • Alternative codes found

    RIV/86652036:_____/23:00570767

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

    SART3 associates with a post-splicing complex

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10601 - Cell biology

Result continuities

  • Project

    <a href="/en/project/GA21-04132S" target="_blank" >GA21-04132S: Molecular mechanism of spliceosomal snRNP formation</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2023

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Cell Science

  • ISSN

    0021-9533

  • e-ISSN

    1477-9137

  • Volume of the periodical

    136

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    11

  • Pages from-to

    jcs260380

  • UT code for WoS article

    000932291900003

  • EID of the result in the Scopus database

    2-s2.0-85147046154