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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/60076658:12310/13:43885294

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

R N A

ISSN

1355-8382

e-ISSN

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Svazek periodika

19

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

649-658

Kód UT WoS článku

000317584100007

EID výsledku v databázi Scopus

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