Essential structural elements in tRNA(Pro) for EF-P-mediated alleviation of translation stalling.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 27216360.
- Also identified by DOI 10.1038/ncomms11657 and PMC identifier 4890201.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Escherichia coli
- Escherichia coli Proteins
- Peptide Elongation Factors
- Protein Biosynthesis
- RNA, Transfer, Pro