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  EF-P is essential for rapid synthesis of proteins containing consecutive proline residues

Doerfel, L. K., Wohlgemuth, I., Kothe, C., Peske, F., Urlaub, H., & Rodnina, M. V. (2013). EF-P is essential for rapid synthesis of proteins containing consecutive proline residues. Science, 339(6115), 85-88. doi:10.1126/science.1229017.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8D55-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E520-1
Genre: Journal Article

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 Creators:
Doerfel, L. K.1, Author              
Wohlgemuth, I.1, Author              
Kothe, C.1, Author              
Peske, F.1, Author              
Urlaub, H.2, Author              
Rodnina, M. V.1, Author              
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: Elongation factor P (EF-P) is a translation factor of unknown function that has been implicated in a great variety of cellular processes. Here, we show that EF-P prevents ribosome from stalling during synthesis of proteins containing consecutive prolines, such as PPG, PPP, or longer proline strings, in natural and engineered model proteins. EF-P promotes peptide-bond formation and stabilizes the peptidyl–transfer RNA in the catalytic center of the ribosome. EF-P is posttranslationally modified by a hydroxylated b-lysine attached to a lysine residue. The modification enhances the catalytic proficiency of the factor mainly by increasing its affinity to the ribosome. We propose that EF-P and its eukaryotic homolog, eIF5A, are essential for the synthesis of a subset of proteins containing proline stretches in all cells.

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Language(s): eng - English
 Dates: 2013-01-04
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1126/science.1229017
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: 339 (6115) Sequence Number: - Start / End Page: 85 - 88 Identifier: -