Translation Elongation Factor EF-P Alleviates Ribosome Stalling at Polyproline Stretches

Author:

Ude Susanne12,Lassak Jürgen12,Starosta Agata L.13,Kraxenberger Tobias12,Wilson Daniel N.13,Jung Kirsten12

Affiliation:

1. Center for Integrated Protein Science Munich (CiPSM), Ludwig-Maximilians-Universität München, Munich, Germany.

2. Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Großhaderner Strasse 2-4, 82152 Martinsried, Germany.

3. Gene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, Feodor-Lynen-Str. 25, 81377 Munich, Germany.

Abstract

Translating Polyproline Translation of messenger RNA into protein is carried out by the ribosome, together with a variety of accessory factors, which offer the potential for regulation of this critical step in gene expression (see the Perspective by Buskirk and Green ). Ude et al. (p. 82 , published online 13 December), using bacterial genetics and an in vitro reconstituted translation system, and Doerfel et al. (p. 85 , published online 13 December), using a model assay for peptide bond formation, find that the universally conserved bacterial elongation factor P (EF-P) (which is orthologous to the archaeal and eukaryotic initiation factor 5A) is required for the efficient translation of polyproline-containing polypeptides. Such short polyproline stretches (with runs of two, three, or more proline residues) would otherwise cause ribosomal stalling.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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