Rorbach 2008 Nucleic Acids Res

From Bioblast
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 36:5787-99.

Β» PMID: 18782833 Open Access

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, UK Newcastle Lightowlers RN


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

Stress:Cell death, Oxidative stress;RONS  Organism: Human 




HRR: Oxygraph-2k 


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