EF-P Is Essential for Rapid Synthesis of Proteins Containing Consecutive Proline Residues

Author:

Doerfel Lili K.1,Wohlgemuth Ingo12,Kothe Christina1,Peske Frank1,Urlaub Henning23,Rodnina Marina V.1

Affiliation:

1. Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany.

2. Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany.

3. Bioanalytics, Department of Clinical Chemistry, University Medical Center Goettingen, 37075 Goettingen, 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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