Structural highlights
Function[A0A1B4WLR4_CORGT] Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.[HAMAP-Rule:MF_00141] Publication Abstract from PubMedTranslation 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. Structure and Function of an Elongation Factor P Subfamily in Actinobacteria.,Pinheiro B, Scheidler CM, Kielkowski P, Schmid M, Forne I, Ye S, Reiling N, Takano E, Imhof A, Sieber SA, Schneider S, Jung K Cell Rep. 2020 Mar 31;30(13):4332-4342.e5. doi: 10.1016/j.celrep.2020.03.009. PMID:32234471[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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