Rorbach 2008 Nucleic Acids Res: Difference between revisions
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{{Publication | {{Publication | ||
|title=Rorbach J, Richter R, Wessels HJ, Wydro M, Pekalski M, Farhoud M, Kühl 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- | |title=Rorbach J, Richter R, Wessels HJ, Wydro M, Pekalski M, Farhoud M, Kühl 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 36:5787-99. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18782833 PMID: 18782833] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/18782833 PMID: 18782833 Open Access] | ||
|authors=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 | |authors=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 | ||
|year=2008 | |year=2008 | ||
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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, UK Newcastle Lightowlers RN | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|area=Respiration, mt-Structure;fission;fusion | |area=Respiration, mt-Structure;fission;fusion | ||
|injuries=Cell death, Oxidative stress;RONS | |||
|organism=Human | |organism=Human | ||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
}} | }} | ||
Latest revision as of 13:42, 27 March 2018
| Rorbach J, Richter R, Wessels HJ, Wydro M, Pekalski M, Farhoud M, Kühl 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 36:5787-99. |
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.
• O2k-Network Lab: NL Nijmegen Koopman WJ, UK Newcastle Lightowlers RN
Labels: MiParea: Respiration, mt-Structure;fission;fusion
Stress:Cell death, Oxidative stress;RONS Organism: Human
HRR: Oxygraph-2k
