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Journal Article

EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons50444

Nierhaus,  Knud H.
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society;

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Tsuboi, M., Morita, H., Nozaki, Y., Akama, K., Ueda, T., Ito, K., et al. (2009). EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis. Molecular Cell, 35(4), 502-510. doi:10.1016/j.molcel.2009.06.028.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-7D24-5
Abstract
Bacterial translation elongation factor G (EF-G) catalyzes translocation during peptide elongation and mediates ribosomal disassembly during ribosome recycling in concert with the ribosomal recycling factor (RRF). Two homologs of EF-G have been identified in mitochondria from yeast to man, EF-G1mt and EF-G2mt. Here, we demonstrate that the dual function of bacterial EF-G is divided between EF-G1mt and EF-G2mt in human mitochondria (RRFmt). EF-G1mt specifically catalyzes translocation, whereas EF-G2mt mediates ribosome recycling with human mitochondrial RRF but lacks translocation activity. Domain swapping experiments suggest that the functional specificity for EF-G2mt resides in domains III and IV. Furthermore, GTP hydrolysis by EF-G2mt is not necessary for ribosomal splitting, in contrast to the bacterial-recycling mode. Because EF-G2mt represents a class of translational GTPase that is involved in ribosome recycling, we propose to rename this factor mitochondrial ribosome recycling factor 2 (RRF2mt).