Rorbach 2008 Nucleic Acids Res

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

» [[Has info::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 ZM (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  Organism: Human, Bacteria 

Regulation: Respiration; OXPHOS; ETS Capacity 

HRR: Oxygraph-2k