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The T. brucei TRM5 methyltransferase plays an essential role in mitochondrial protein synthesis and function

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F13%3A00420979" target="_blank" >RIV/60077344:_____/13:00420979 - isvavai.cz</a>

  • Alternative codes found

    RIV/60076658:12310/13:43885294

  • Result on the web

    <a href="http://dx.doi.org/10.1261/rna.036665.112" target="_blank" >http://dx.doi.org/10.1261/rna.036665.112</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1261/rna.036665.112" target="_blank" >10.1261/rna.036665.112</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The T. brucei TRM5 methyltransferase plays an essential role in mitochondrial protein synthesis and function

  • Original language description

    All tRNAs undergo post-transcriptional chemical modifications as part of their natural maturation pathway. Some modifications, especially those in the anticodon loop, play important functions in translational efficiency and fidelity. Among these, 1-methylguanosine, at position 37 (m(1)G(37)) of the anticodon loop in several tRNAs, is evolutionarily conserved and participates in translational reading frame maintenance. In eukaryotes, the tRNA methyltransferase TRM5 is responsible for m(1)G formation in nucleus-encoded as well as mitochondria-encoded tRNAs, reflecting the universal importance of this modification for protein synthesis. However, it is not clear what role, if any, mitochondrial TRM5 serves in organisms that do not encode tRNAs in their mitochondrial genomes. These organisms may easily satisfy the m(1)G(37) requirement through their robust mitochondrial tRNA import mechanisms. We have explored this possibility in the parasitic protist Trypanosoma brucei and show that down-r

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

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

    2013

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    R N A

  • ISSN

    1355-8382

  • e-ISSN

  • Volume of the periodical

    19

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    649-658

  • UT code for WoS article

    000317584100007

  • EID of the result in the Scopus database