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

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.

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Genre: Zeitschriftenartikel
Alternativer Titel : Mol Cell

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 Urheber:
Tsuboi, Masafumi, Autor
Morita, Hiroyuki, Autor
Nozaki, Yusuke, Autor
Akama, Kenta, Autor
Ueda, Takuya, Autor
Ito, Koichi, Autor
Nierhaus, Knud H.1, Autor           
Takeuchi, Nono, Autor
Affiliations:
1Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              

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Schlagwörter: Proteins; RNA
 Zusammenfassung: 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).

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Sprache(n): eng - English
 Datum: 2009-08-28
 Publikationsstatus: Erschienen
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Titel: Molecular Cell
  Alternativer Titel : Mol Cell
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 35 (4) Artikelnummer: - Start- / Endseite: 502 - 510 Identifikator: ISSN: 1097-2765