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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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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7D24-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7D25-3
Genre: Journal Article
Alternative Title : Mol Cell

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

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Free keywords: Proteins; RNA
 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).

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Language(s): eng - English
 Dates: 2009-08-28
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Degree: -

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Title: Molecular Cell
  Alternative Title : Mol Cell
Source Genre: Journal
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Pages: - Volume / Issue: 35 (4) Sequence Number: - Start / End Page: 502 - 510 Identifier: ISSN: 1097-2765