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  A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation

Connell, S. R., Topf, M., Qin, Y., Wilson, D. N., Mielke, T., Fucini, P., et al. (2008). A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation. Nature Structural & Molecular Biology, 15(9), 910-915. doi:10.1038/nsmb.1469.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7F2D-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7F2E-E
Genre: Journal Article
Alternative Title : Nat Struct Mol Biol

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 Creators:
Connell, Sean R.1, Author              
Topf, Maya, Author
Qin, Yan2, Author              
Wilson, Daniel N.1, Author              
Mielke, Thorsten3, Author              
Fucini, Paola2, Author              
Nierhaus, Knud H.2, Author              
Spahn, Christian M. T.1, Author              
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              
3Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

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 Abstract: EF4 (LepA) is an almost universally conserved translational GTPase in eubacteria. It seems to be essential under environmental stress conditions and has previously been shown to back-translocate the tRNAs on the ribosome, thereby reverting the canonical translocation reaction. In the current work, EF4 was directly visualized in the process of back-translocating tRNAs by single-particle cryo-EM. Using flexible fitting methods, we built a model of ribosome-bound EF4 based on the cryo-EM map and a recently published unbound EF4 X-ray structure. The cryo-EM map establishes EF4 as a noncanonical elongation factor that interacts not only with the elongating ribosome, but also with the back-translocated tRNA in the A-site region, which is present in a previously unseen, intermediate state and deviates markedly from the position of a canonical A-tRNA. Our results, therefore, provide insight into the underlying structural principles governing back-translocation.

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Language(s): eng - English
 Dates: 2008-09
 Publication Status: Published in print
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Title: Nature Structural & Molecular Biology
  Alternative Title : Nat Struct Mol Biol
Source Genre: Journal
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Pages: - Volume / Issue: 15 (9) Sequence Number: - Start / End Page: 910 - 915 Identifier: ISSN: 1545-9993