Structure and Function of an Elongation Factor P Subfamily in Actinobacteria
| Autor: | Stephan A. Sieber, Christopher M. Scheidler, Eriko Takano, Pavel Kielkowski, Sabine Schneider, Kirsten Jung, Norbert Reiling, Suhui Ye, Ignasi Forné, Marina Schmid, Axel Imhof, Bruno Pinheiro |
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| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Models Molecular Proteomics Translation Subfamily Amino Acid Motifs Streptomyces coelicolor Crystallography X-Ray Streptomyces General Biochemistry Genetics and Molecular Biology Actinobacteria 03 medical and health sciences Structure-Activity Relationship 0302 clinical medicine Bacterial Proteins Amino Acid Sequence Amino Acids Conserved Sequence Phylogeny EF-P biology Translation (biology) Mycobacterium tuberculosis biology.organism_classification Peptide Elongation Factors Corynebacterium glutamicum 030104 developmental biology Biochemistry Elongation factor P bacteria Post-translational modification EIF5A Protein Processing Post-Translational 030217 neurology & neurosurgery Bacteria Mycobacterium |
| Zdroj: | Cell Reports Pinheiro, B, Scheidler, C, Kielkowski, P, Schmid, M, Forne, I, Ye Huang, S, Reiling, N, Takano, E, Imhof, A, Sieber, S, Schneider, S & Jung, K 2020, ' Structure and function of a novel elongation factor P subfamily in Actinobacteria ', Cell Reports . https://doi.org/10.1016/j.celrep.2020.03.009 |
| ISSN: | 2211-1247 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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