Evidence map›Paper›PMID 28715177›Full record

ArticleBiochemistry2017

Ribosome Mediated Quinary Interactions Modulate In-Cell Protein Activities.

Christopher M DeMott, Subhabrata Majumder, David S Burz, Sergey Reverdatto, Alexander Shekhtman

Abstract read
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. RNA Structure: Past, Future, and Gene Therapy Applications.International journal of molecular sciences · 2024
    Review
  5. Article
  6. Review
  7. Article
  8. Common sequence motifs of nascent chains engage the ribosome surface and trigger factor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. An in vitro mimic of in-cell solvation for protein folding studies.Protein science : a publication of the Protein Society · 2020
    Article
  14. Article
  15. International journal of molecular sciences · 2019
    Review
  16. Review
  17. Article
  18. 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

5 authors at 1 institution in 1 country.

Christopher M DeMottDepartment of Chemistry, State University of New York at Albany , Albany, New York 12222, United States.
Subhabrata MajumderDepartment of Chemistry, State University of New York at Albany , Albany, New York 12222, United States.
David S BurzDepartment of Chemistry, State University of New York at Albany , Albany, New York 12222, United States.
Sergey ReverdattoDepartment of Chemistry, State University of New York at Albany , Albany, New York 12222, United States.
Alexander ShekhtmanDepartment of Chemistry, State University of New York at Albany , Albany, New York 12222, United States.ORCID 0000-0003-2649-2675
University at Albany, State University of New York · US

Funding

Real Time (RT) In-cell NMR technology to study protein interactions in live cellsR01GM085006 · NIGMS · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI SHEKHTMAN, ALEXANDER · 2010 to 2021
$2.4M
NIGMS NIH HHS R01 GM085006
6 · The paper itself

Abstract

Ribosomes are present inside bacterial cells at micromolar concentrations and occupy up to 20% of the cell volume. Under these conditions, even weak quinary interactions between ribosomes and cytosolic proteins can affect protein activity. By using in-cell and in vitro NMR spectroscopy, and biophysical techniques, we show that the enzymes, adenylate kinase and dihydrofolate reductase, and the respective coenzymes, ATP and NADPH, bind to ribosomes with micromolar affinity, and that this interaction suppresses the enzymatic activities of both enzymes. Conversely, thymidylate synthase, which works together with dihydrofolate reductase in the thymidylate synthetic pathway, is activated by ribosomes. We also show that ribosomes impede diffusion of green fluorescent protein in vitro and contribute to the decrease in diffusion in vivo. These results strongly suggest that ribosome-mediated quinary interactions contribute to the differences between in vitro and in vivo protein activities and that ribosomes play a previously under-appreciated nontranslational role in regulating cellular biochemistry.

Indexed as

Adenosine TriphosphateAdenylate KinaseCoenzymesEscherichia coliEscherichia coli ProteinsGreen Fluorescent ProteinsNADPNuclear Magnetic Resonance, BiomolecularRibosomesTetrahydrofolate DehydrogenaseAdenosine TriphosphateAdenylate KinaseCoenzymesEscherichia coli ProteinsGreen Fluorescent ProteinsNADPTetrahydrofolate Dehydrogenase

Identifiers

PMID28715177
PMCPMC5956540
OpenAlexW2735014630

What OpenQuestion holds

Textmetadata
LicenceTDM
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.