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Aim-less translation : Loss of Saccharomyces cerevisiae mitochondrial translation initiation factor mIF3/Aim23 leads to unbalanced protein synthesis

Kuzmenko, Anton ; Derbikova, Ksenia ; Salvatori, Roger ; Tankov, Stoyan ; Atkinson, Gemma C. LU ; Tenson, Tanel ; Ott, Martin ; Kamenski, Piotr and Hauryliuk, Vasili LU orcid (2016) In Scientific Reports 6.
Abstract

The mitochondrial genome almost exclusively encodes a handful of transmembrane constituents of the oxidative phosphorylation (OXPHOS) system. Coordinated expression of these genes ensures the correct stoichiometry of the system's components. Translation initiation in mitochondria is assisted by two general initiation factors mIF2 and mIF3, orthologues of which in bacteria are indispensible for protein synthesis and viability. mIF3 was thought to be absent in Saccharomyces cerevisiae until we recently identified mitochondrial protein Aim23 as the missing orthologue. Here we show that, surprisingly, loss of mIF3/Aim23 in S. cerevisiae does not indiscriminately abrogate mitochondrial translation but rather causes an imbalance in protein... (More)

The mitochondrial genome almost exclusively encodes a handful of transmembrane constituents of the oxidative phosphorylation (OXPHOS) system. Coordinated expression of these genes ensures the correct stoichiometry of the system's components. Translation initiation in mitochondria is assisted by two general initiation factors mIF2 and mIF3, orthologues of which in bacteria are indispensible for protein synthesis and viability. mIF3 was thought to be absent in Saccharomyces cerevisiae until we recently identified mitochondrial protein Aim23 as the missing orthologue. Here we show that, surprisingly, loss of mIF3/Aim23 in S. cerevisiae does not indiscriminately abrogate mitochondrial translation but rather causes an imbalance in protein production: the rate of synthesis of the Atp9 subunit of F1F0 ATP synthase (complex V) is increased, while expression of Cox1, Cox2 and Cox3 subunits of cytochrome c oxidase (complex IV) is repressed. Our results provide one more example of deviation of mitochondrial translation from its bacterial origins.

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Contribution to journal
publication status
published
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in
Scientific Reports
volume
6
article number
18749
publisher
Nature Publishing Group
external identifiers
  • pmid:26728900
  • scopus:84953249297
ISSN
2045-2322
DOI
10.1038/srep18749
language
English
LU publication?
no
additional info
Funding Information: We are grateful to Ivan Tarassov and Nina Entelis (University of Strasbourg, France), Thomas D. Fox (Cornell University, USA), Roland Lill (University of Marburg, Germany), Marie-France Giraud (University of Bordeaux, France) and Konstantin Khodosevich (University of Heidelberg, Germany) for sharing strains and materials, to Michael Vyssokikh (Research Center of Obstetrics, Gynecology, and Perinatology, Moscow, Russia) for help with oxymetry and to Sergey Levitsky (Moscow State University, Russia) and Marcus Johansson (Umeå University) for helpful discussions. This work was supported by the European Regional Development Fund through the Centre of Excellence in Chemical Biology (VH and TT); Estonian Science Foundation (grants ETF9012 and PUT37 to VH, ETF9020 to GCA); Umeå University, the Swedish Research council Vetenskapsrådet (grant 2013–4680), Kempe and Ragnar Söderberg foundations (VH); the Swedish research council Vetenskapsrådet (grant 2010–4613), the Center for Biomembrane Research at Stockholm University, the Carl Tryggers foundation, and the Knut and Alice Wallenberg Foundation (MO); the Archimedes Foundation (ST and AK); and the Russian Foundation for Basic Research (grants 14-04-31008 and 15-34-20124 to AK, KD and PK). Studies of mitochondrial translation at Moscow State University were supported by Russian Science Foundation (grant 14-50-00029 to PK). Publisher Copyright: © 2015, Nature Publishing Group. All rights reserved. Copyright: Copyright 2018 Elsevier B.V., All rights reserved.
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b28da008-aa75-4481-bd7c-98b506fbe4e6
date added to LUP
2021-09-24 20:44:14
date last changed
2024-02-20 13:12:25
@article{b28da008-aa75-4481-bd7c-98b506fbe4e6,
  abstract     = {{<p>The mitochondrial genome almost exclusively encodes a handful of transmembrane constituents of the oxidative phosphorylation (OXPHOS) system. Coordinated expression of these genes ensures the correct stoichiometry of the system's components. Translation initiation in mitochondria is assisted by two general initiation factors mIF2 and mIF3, orthologues of which in bacteria are indispensible for protein synthesis and viability. mIF3 was thought to be absent in Saccharomyces cerevisiae until we recently identified mitochondrial protein Aim23 as the missing orthologue. Here we show that, surprisingly, loss of mIF3/Aim23 in S. cerevisiae does not indiscriminately abrogate mitochondrial translation but rather causes an imbalance in protein production: the rate of synthesis of the Atp9 subunit of F<sub>1</sub>F<sub>0</sub> ATP synthase (complex V) is increased, while expression of Cox1, Cox2 and Cox3 subunits of cytochrome c oxidase (complex IV) is repressed. Our results provide one more example of deviation of mitochondrial translation from its bacterial origins.</p>}},
  author       = {{Kuzmenko, Anton and Derbikova, Ksenia and Salvatori, Roger and Tankov, Stoyan and Atkinson, Gemma C. and Tenson, Tanel and Ott, Martin and Kamenski, Piotr and Hauryliuk, Vasili}},
  issn         = {{2045-2322}},
  language     = {{eng}},
  month        = {{01}},
  publisher    = {{Nature Publishing Group}},
  series       = {{Scientific Reports}},
  title        = {{Aim-less translation : Loss of Saccharomyces cerevisiae mitochondrial translation initiation factor mIF3/Aim23 leads to unbalanced protein synthesis}},
  url          = {{http://dx.doi.org/10.1038/srep18749}},
  doi          = {{10.1038/srep18749}},
  volume       = {{6}},
  year         = {{2016}},
}