Rorbach 2008 Nucleic Acids Res: Difference between revisions

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Expression of human mtRRF in fission yeast devoid of endogenous mitochondrial Recycling factor suppresses the respiratory phenotype. Further, human mtRRF is able to associate with ''Escherichia coli'' ribosomes ''in vitro'' and can associate with mitoribosomes ''in vivo''. Depletion of mtRRF in human cell lines is lethal, initially causing profound mitochondrial dysmorphism, aggregation of mitoribosomes, elevated mitochondrial superoxide production
Expression of human mtRRF in fission yeast devoid of endogenous mitochondrial Recycling factor suppresses the respiratory phenotype. Further, human mtRRF is able to associate with ''Escherichia coli'' ribosomes ''in vitro'' and can associate with mitoribosomes ''in vivo''. Depletion of mtRRF in human cell lines is lethal, initially causing profound mitochondrial dysmorphism, aggregation of mitoribosomes, elevated mitochondrial superoxide production
and eventual loss of OXPHOS complexes. Finally, mtRRF was shown to co-immunoprecipitate a large number of mitoribosomal proteins attached
and eventual loss of OXPHOS complexes. Finally, mtRRF was shown to co-immunoprecipitate a large number of mitoribosomal proteins attached
to other mitochondrial proteins, including
to other mitochondrial proteins, including putative members of the mt-nucleoid.
|mipnetlab=NL Nijmegen Koopman WJ
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{{Labeling

Revision as of 14:59, 12 August 2013

Publications in the MiPMap
Rorbach J, Richter R, Wessels HJ, Wydro M, Pekalski M, Farhoud M, KΓΌhl I, Gaisne M, Bonnefoy N, Smeitink JA, Lightowlers RN, Chrzanowska-Lightowlers ZMA (2008) The human mitochondrial ribosome recycling factor is essential for cell viability. Nucleic Acids Res 36: 5787-5799.

Β» PMID: 18782833

Rorbach J, Richter R, Wessels HJ, Wydro M, Pekalski M, Farhoud M, Kuehl I, Gaisne M, Bonnefoy N, Smeitink JA, Lightowlers RN, Chrzanowska-Lightowlers ZMA (2008) Nucleic Acids Res

Abstract: The molecular mechanism of human mitochondrial translation has yet to be fully described. We are particularly interested in understanding the process of translational termination and ribosome recycling in the mitochondrion. Several candidates have been implicated, for which subcellular localization and characterization have not been reported. Here, we show that the putative mitochondrial Recycling factor, mtRRF, is indeed a mitochondrial protein. Expression of human mtRRF in fission yeast devoid of endogenous mitochondrial Recycling factor suppresses the respiratory phenotype. Further, human mtRRF is able to associate with Escherichia coli ribosomes in vitro and can associate with mitoribosomes in vivo. Depletion of mtRRF in human cell lines is lethal, initially causing profound mitochondrial dysmorphism, aggregation of mitoribosomes, elevated mitochondrial superoxide production and eventual loss of OXPHOS complexes. Finally, mtRRF was shown to co-immunoprecipitate a large number of mitoribosomal proteins attached to other mitochondrial proteins, including putative members of the mt-nucleoid.


β€’ O2k-Network Lab: NL Nijmegen Koopman WJ


Labels: MiParea: Respiration, mt-Structure;fission;fusion 

Stress:Cell death, RONS; Oxidative Stress"RONS; Oxidative Stress" is not in the list (Cell death, Cryopreservation, Ischemia-reperfusion, Permeability transition, Oxidative stress;RONS, Temperature, Hypoxia, Mitochondrial disease) of allowed values for the "Stress" property., Genetic Defect; Knockdown; Overexpression"Genetic Defect; Knockdown; Overexpression" is not in the list (Cell death, Cryopreservation, Ischemia-reperfusion, Permeability transition, Oxidative stress;RONS, Temperature, Hypoxia, Mitochondrial disease) of allowed values for the "Stress" property.  Organism: Human 




HRR: Oxygraph-2k 


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