de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

The Highly Conserved LepA Is a Ribosomal Elongation Factor that Back-Translocates the Ribosome

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons50475

Qin,  Yan
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50610

Vesper,  Oliver
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society;

Staub,  Eike
Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50143

Einfeldt,  Edda
Mechanisms of Transcriptional Regulation (Sebastiaan H. Meijsing), Dept. of Computational Molecular Biology (Head: Martin Vingron), Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50642

Wilson,  Daniel N.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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

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

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Qin, Y., Polacek, N., Vesper, O., Staub, E., Einfeldt, E., Wilson, D. N., et al. (2006). The Highly Conserved LepA Is a Ribosomal Elongation Factor that Back-Translocates the Ribosome. Cell, 127(4), 721-733. doi:10.1016/j.cell.2006.09.037.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-8336-A
Abstract
The ribosomal elongation cycle describes a series of reactions prolonging the nascent polypeptide chain by one amino acid and driven by two universal elongation factors termed EF-Tu and EF-G in bacteria. Here we demonstrate that the extremely conserved LepA protein, present in all bacteria and mitochondria, is a third elongation factor required for accurate and efficient protein synthesis. LepA has the unique function of back-translocating posttranslocational ribosomes, and the results suggest that it recognizes ribosomes after a defective translocation reaction and induces a back-translocation, thus giving EF-G a second chance to translocate the tRNAs correctly. We suggest renaming LepA as elongation factor 4 (EF4).