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Key RNA-binding domains in the La protein establish tRNA modification levels in Trypanosoma brucei

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F25%3A00637548" target="_blank" >RIV/60077344:_____/25:00637548 - isvavai.cz</a>

  • Alternative codes found

    RIV/60076658:12310/25:43910296

  • Result on the web

    <a href="https://doi.org/10.1093/nar/gkaf594" target="_blank" >https://doi.org/10.1093/nar/gkaf594</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1093/nar/gkaf594" target="_blank" >10.1093/nar/gkaf594</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Key RNA-binding domains in the La protein establish tRNA modification levels in Trypanosoma brucei

  • Original language description

    The RNA-binding protein La is found in most eukaryotes, and despite being essential in many organisms, its function is not completely clear. Trypanosoma brucei, the causative agent of human African trypanosomiasis, encodes a 'classical' La protein (TbLa) composed of a La-motif, two RNA recognition motifs (RRM1 and RRM2 alpha), a C-terminal short basic motif (SBM), and a nuclear localization signal (NLS). In T. brucei, like in most eukaryotes, position 34 of tRNATyr,Asp,Asn andHis is modified with queuosine (Q34). The steady-state levels of queuosine-modified tRNA in the insect form (procyclic) of T. brucei can fluctuate dynamically depending on growth conditions, but the mechanism(s) controlling Q34 levels are not well understood. A well-established function of La is in precursor-tRNA 3 '-end metabolism, but in this work, we demonstrate that La also controls Q34-tRNA levels. Individual domain deletions showed that while deletion of La motif or RRM1 causes dysregulation of Q34-tRNA levels, no other domain plays a similar role. We also show that La is important for the normal balance of several additional tRNA modifications. These findings are discussed in the context of substrate competition between La and modification enzymes, also highlighting subcellular localization as a key determinant of tRNA function.

  • 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

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2025

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Nucleic Acids Research

  • ISSN

    0305-1048

  • e-ISSN

    1362-4962

  • Volume of the periodical

    53

  • Issue of the periodical within the volume

    13

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    16

  • Pages from-to

    gkaf594

  • UT code for WoS article

    001525153800001

  • EID of the result in the Scopus database

    2-s2.0-105010623488