Rorbach 2008 Nucleic Acids Res: Difference between revisions
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|year=2008 | |year=2008 | ||
|journal=Nucleic Acids Res | |journal=Nucleic Acids Res | ||
|abstract=The molecular mechanism of human mitochondrial | |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. | ||
translation has yet to be fully described. We are particularly | 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 | ||
interested in understanding the process of | and eventual loss of OXPHOS complexes. Finally, mtRRF was shown to co-immunoprecipitate a large number of mitoribosomal proteins attached | ||
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 | |||
factor, mtRRF, is indeed a mitochondrial protein. | |||
Expression of human mtRRF in fission yeast | |||
devoid of endogenous mitochondrial | |||
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 | to other mitochondrial proteins, including | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism=Human | |||
|injuries=Genetic Defect; Knockdown; Overexpression | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
}} | }} |
Revision as of 17:27, 8 August 2013
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. |
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
Labels:
Stress: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