Evidence map›Paper›PMID 23277358›Full record

ArticleThe Journal of biological chemistry2013

(R)-β-lysine-modified elongation factor P functions in translation elongation.

Tammy J Bullwinkle, S Betty Zou, Andrei Rajkovic, Steven J Hersch, Sara Elgamal, Nathaniel Robinson, David Smil, Yuri Bolshan, William Wiley Navarre, Michael Ibba

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 53 citations in OpenAlex.

  1. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Unravelling the sexual developmental biology ofFrontiers in cellular and infection microbiology · 2023
    Article
  8. Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021
    Review
  9. Review
  10. Article
  11. Article
  12. Ribosome collisions alter frameshifting at translational reprogramming motifs in bacterial mRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Elongation factor P is required to maintain proteome homeostasis at high growth rate.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Rewiring protein synthesis: From natural to synthetic amino acids.Biochimica et biophysica acta. General subjects · 2017
    Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 2 countries.

Tammy J BullwinkleDepartment of Microbiology, Ohio State University, Columbus, Ohio 43210, USA.
S Betty Zou
Andrei Rajkovic
Steven J Hersch
Sara Elgamal
Nathaniel Robinson
David Smil
Yuri Bolshan
William Wiley Navarre
Michael Ibba
The Ohio State University · USUniversity of Toronto · CAStructural Genomics Consortium · CA

Funding

Mechanisms of translational controlR01GM065183 · NIGMS · OHIO STATE UNIVERSITY · PI DUNHAM, CHRISTINE M, FREDRICK, KURT L · 2003 to 2020
$4.9M
CIHR MOP-86683CIHR MSH-87729NIGMS NIH HHS GM 65183NIGMS NIH HHS R01 GM065183
6 · The paper itself

Abstract

Post-translational modification of bacterial elongation factor P (EF-P) with (R)-β-lysine at a conserved lysine residue activates the protein in vivo and increases puromycin reactivity of the ribosome in vitro. The additional hydroxylation of EF-P at the same lysine residue by the YfcM protein has also recently been described. The roles of modified and unmodified EF-P during different steps in translation, and how this correlates to its physiological role in the cell, have recently been linked to the synthesis of polyproline stretches in proteins. Polysome analysis indicated that EF-P functions in translation elongation, rather than initiation as proposed previously. This was further supported by the inability of EF-P to enhance the rate of formation of fMet-Lys or fMet-Phe, indicating that the role of EF-P is not to specifically stimulate formation of the first peptide bond. Investigation of hydroxyl-(β)-lysyl-EF-P showed 30% increased puromycin reactivity but no differences in dipeptide synthesis rates when compared with the β-lysylated form. Unlike disruption of the other genes required for EF-P modification, deletion of yfcM had no phenotypic consequences in Salmonella. Taken together, our findings indicate that EF-P functions in translation elongation, a role critically dependent on post-translational β-lysylation but not hydroxylation.

Indexed as

Bacterial ProteinsEscherichia coliHydroxylationLysineMixed Function OxygenasesPeptide Chain Elongation, TranslationalPeptide Elongation FactorsProtein Processing, Post-TranslationalSalmonella entericaBacterial Proteinsfactor EF-PLysineMixed Function OxygenasesPeptide Elongation Factors

Identifiers

PMID23277358
PMCPMC3567691
OpenAlexW1978635623

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.