Essential Structural Elements in TRNA(Pro) for EF-P-mediated Alleviation of Translation Stalling

Overview

Journal Nat Commun

Specialty Biology

Date 2016 May 25

PMID 27216360

Citations 44

Authors

Takayuki Katoh

Ingo Wohlgemuth

Masanobu Nagano

Marina V Rodnina

Hiroaki Suga

Affiliations

Soon will be listed here.

Abstract

The ribosome stalls on translation of polyproline sequences due to inefficient peptide bond formation between consecutive prolines. The translation factor EF-P is able to alleviate this stalling by accelerating Pro-Pro formation. However, the mechanism by which EF-P recognizes the stalled complexes and accelerates peptide bond formation is not known. Here, we use genetic code reprogramming through a flexible in-vitro translation (FIT) system to investigate how mutations in tRNA(Pro) affect EF-P function. We show that the 9-nt D-loop closed by the stable D-stem sequence in tRNA(Pro) is a crucial recognition determinant for EF-P. Such D-arm structures are shared only among the tRNA(Pro) isoacceptors and tRNA(fMet) in Escherichia coli, and the D-arm of tRNA(fMet) is essential for EF-P-induced acceleration of fMet-puromycin formation. Thus, the activity of EF-P is controlled by recognition elements in the tRNA D-arm.

Citing Articles

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EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences.

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Kinetic mechanism and determinants of EF-P recruitment to translating ribosomes.

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The human mitochondrial translation factor TACO1 alleviates mitoribosome stalling at polyproline stretches.

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