TY  - INPR
A1  - Sieber, Alina Maria
A1  - Parr, Marina
A1  - Ehr, Julian von
A1  - Dhamotharan, Karthikeyan
A1  - Kielkowski, Pavel
A1  - Brewer, Tess
A1  - Schaepers, Anna
A1  - Krafczyk, Ralph
A1  - Qi, Fei
A1  - Schlundt, Andreas
A1  - Frishman, Dmitrij
A1  - Lassak, Jürgen
T1  - EF-P and its paralog EfpL (YeiP) differentially control translation of proline containing sequences
T2  - bioRxiv
N2  - Polyproline sequences (XPPX) stall ribosomes, thus being deleterious for all living organisms. In bacteria, translation elongation factor P (EF-P) plays a crucial role in overcoming such arrests. 12% of eubacteria possess an EF-P paralog – YeiP (EfpL) of unknown function. Here, we functionally and structurally characterize EfpL from Escherichia coli and demonstrate its yet unrecognized role in the translational stress response. Through ribosome profiling, we analyzed the EfpL arrest motif spectrum and discovered additional stalls beyond the canonical XPPX motifs at single-proline sequences (XPX), that both EF-P and EfpL can resolve. Notably, the two factors can also induce pauses. We further report that, contrary to the housekeeping EF-P, EfpL can sense the metabolic state of the cell, via lysine acylation. Together, our work uncovers a new player 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.
Y1  - 2024
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/83810
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-838101
UR  - https://www.biorxiv.org/content/10.1101/2024.04.15.589488v1
IS  - 2024.04.15.589488 Version 1
PB  - bioRxiv
ER  -