8S8U

Escherichia coli translation elongation factor P like protein (EfpL)

Summary for 8S8U

• Entry DOI: 10.2210/pdb8s8u/pdb
• Descriptor: Elongation factor P-like protein (2 entities in total)
• Functional Keywords: ef-p like, yeip, polyproline translation, translation
• Biological source: Escherichia coli K-12
• Total number of polymer chains: 2
• Total formula weight: 43026.99

Authors

Dhamotharan, K.,von Ehr, J.,Schlundt, A.,Lassak, J. (deposition date: 2024-03-07, release date: 2024-10-09, Last modification date: 2024-12-11)

Primary citation

Sieber, A.,Parr, M.,von Ehr, J.,Dhamotharan, K.,Kielkowski, P.,Brewer, T.,Schapers, A.,Krafczyk, R.,Qi, F.,Schlundt, A.,Frishman, D.,Lassak, J.
EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences.
Nat Commun, 15:10465-10465, 2024

PubMed Abstract: Polyproline sequences are deleterious to cells because they stall ribosomes. In bacteria, EF-P plays an important role in overcoming such polyproline sequence-induced ribosome stalling. Additionally, numerous bacteria possess an EF-P paralog called EfpL (also known as YeiP) of unknown function. Here, we functionally and structurally characterize EfpL from Escherichia coli and demonstrate its role in the translational stress response. Through ribosome profiling, we analyze the EfpL arrest motif spectrum and find additional sequences beyond the canonical polyproline motifs that both EF-P and EfpL can resolve. Notably, the two factors can also induce pauses. We further report that EfpL can sense the metabolic state of the cell via lysine acylation. Overall, our work characterizes the role of EfpL in ribosome rescue at proline-containing sequences, and provides evidence that co-occurrence of EF-P and EfpL is an evolutionary driver for higher bacterial growth rates.

PubMed: 39622818
DOI: 10.1038/s41467-024-54556-9

Experimental method

X-RAY DIFFRACTION (2.27 Å)