EF-G2mt Is an Exclusive Recycling Factor in Mammalian Mitochondrial Protein Synthesis
EF-G2mt Is an Exclusive Recycling Factor in Mammalian Mitochondrial Protein Synthesis
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DOI:
10.1016/j.molcel.2009.06.028
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发表时间:
2009-08-28
期刊:
影响因子:
16
通讯作者:
Takeuchi, Nono
中科院分区:
文献类型:
--
作者:
Tsuboi, Masafumi;Morita, Hiroyuki;Takeuchi, Nono
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).