Structure and Function of an Elongation Factor P Subfamily in Actinobacteria.

Bruno Pinheiro, Christopher M Scheidler, Pavel Kielkowski, Marina Schmid, Ignasi Forné, Suhui Ye, Norbert Reiling, Eriko Takano, Axel Imhof, Stephan A Sieber, Sabine Schneider, Kirsten Jung

Cell reports 2020 Mar 31

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Translation of consecutive proline motifs causes ribosome stalling and requires rescue via the action of a specific translation elongation factor, EF-P in bacteria and archaeal/eukaryotic a/eIF5A. In Eukarya, Archaea, and all bacteria investigated so far, the functionality of this translation elongation factor depends on specific and rather unusual post-translational modifications. The phylum Actinobacteria, which includes the genera Corynebacterium, Mycobacterium, and Streptomyces, is of both medical and economic significance. Here, we report that EF-P is required in these bacteria in particular for the translation of proteins involved in amino acid and secondary metabolite production. Notably, EF-P of Actinobacteria species does not need any post-translational modification for activation. While the function and overall 3D structure of this EF-P type is conserved, the loop containing the conserved lysine is flanked by two essential prolines that rigidify it. Actinobacteria's EF-P represents a unique subfamily that works without any modification. Copyright © 2020 The Author(s). Published by Elsevier Inc. All rights reserved.

Citation

Bruno Pinheiro, Christopher M Scheidler, Pavel Kielkowski, Marina Schmid, Ignasi Forné, Suhui Ye, Norbert Reiling, Eriko Takano, Axel Imhof, Stephan A Sieber, Sabine Schneider, Kirsten Jung. Structure and Function of an Elongation Factor P Subfamily in Actinobacteria. Cell reports. 2020 Mar 31;30(13):4332-4342.e5