Evidence map›Paper›PMID 34652913›Full record

ArticleBiochemistry2021

Ribosome Elongation Kinetics of Consecutively Charged Residues Are Coupled to Electrostatic Force.

Sarah E Leininger, Judith Rodriguez, Quyen V Vu, Yang Jiang, Mai Suan Li, Carol Deutsch, Edward P O'Brien

Erratum issuedAbstract read
In one paragraph

Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Translation Rates and Protein Folding.Journal of molecular biology · 2024
    Review
  7. Article
  8. How the ribosome shapes cotranslational protein folding.Current opinion in structural biology · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Sarah E LeiningerDepartment of Chemistry, Penn State University, University Park, Pennsylvania 16802, United States.ORCID 0000-0002-9663-9700
Judith RodriguezBioinformatics and Genomics Graduate Program, Huck Institutes of the Life Sciences, Penn State University, University Park, Pennsylvania 16802, United States.
Quyen V VuInstitute of Physics, Polish Academy of Sciences, Warsaw 02-668, Poland.ORCID 0000-0002-9863-0486
Yang JiangDepartment of Chemistry, Penn State University, University Park, Pennsylvania 16802, United States.
Mai Suan LiInstitute of Physics, Polish Academy of Sciences, Warsaw 02-668, Poland.ORCID 0000-0001-7021-7916
Carol DeutschDepartment of Physiology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Edward P O'BrienDepartment of Chemistry, Penn State University, University Park, Pennsylvania 16802, United States.ORCID 0000-0001-9809-3273

Funding

FUNCTION AND ASSEMBLY OF POTASSIUM CHANNELSR01GM052302 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEUTSCH, CAROL J · 1995 to 2024
$13.4M
Translation Kinetics and their Effects on Protein Structure and Function, mRNA half-lives, and Cellular PhenotypeR35GM124818 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI Edward Patrick O'Brien · 2017 to 2026
$4.0M
NIGMS NIH HHS R01 GM052302NIGMS NIH HHS R35 GM124818
6 · The paper itself

Abstract

The speed of protein synthesis can dramatically change when consecutively charged residues are incorporated into an elongating nascent protein by the ribosome. The molecular origins of this class of allosteric coupling remain unknown. We demonstrate, using multiscale simulations, that positively charged residues generate large forces that move the P-site amino acid away from the A-site amino acid. Negatively charged residues generate forces of similar magnitude but move the A- and P-sites closer together. These conformational changes, respectively, increase and decrease the transition state barrier height to peptide bond formation, explaining how charged residues mechanochemically alter translation speed. This mechanochemical mechanism is consistent with

Indexed as

Amino AcidsKineticsModels, ChemicalModels, TheoreticalProtein BiosynthesisProtein ConformationRibosomesStatic ElectricityAmino Acids

Identifiers

PMID34652913
PMCPMC8916236

What OpenQuestion holds

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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.