Evidence map›Paper›PMID 25982410›Full record

ArticleBiochemistry2015

Protein Synthesis with Ribosomes Selected for the Incorporation of β-Amino Acids.

Rumit Maini, Sandipan Roy Chowdhury, Larisa M Dedkova, Basab Roy, Sasha M Daskalova, Rakesh Paul, Shengxi Chen, Sidney M Hecht

Abstract read
In one paragraph

Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Biological Regulation StudiedAccounts of chemical research · 2025
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  4. RNA language models predict mutations that improve RNA function.bioRxiv : the preprint server for biology · 2024
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  6. Engineered mRNA-ribosome fusions for facile biosynthesis of selenoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Cell-free Biosynthesis of Peptidomimetics.Biotechnology and bioprocess engineering : BBE · 2023
    Review
  9. Article
  10. Article
  11. In Vitro Selection of Macrocyclic α/βJournal of the American Chemical Society · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Reprogramming the genetic code.Nature reviews. Genetics · 2021
    Review
  18. Article
  19. Article
  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

8 authors at 2 institutions in 1 country.

Rumit MainiCenter for BioEnergetics, Biodesign Institute, and Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287, United States.
Sandipan Roy ChowdhuryCenter for BioEnergetics, Biodesign Institute, and Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287, United States.
Larisa M DedkovaCenter for BioEnergetics, Biodesign Institute, and Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287, United States.
Basab RoyCenter for BioEnergetics, Biodesign Institute, and Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287, United States.
Sasha M DaskalovaCenter for BioEnergetics, Biodesign Institute, and Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287, United States.
Rakesh PaulCenter for BioEnergetics, Biodesign Institute, and Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287, United States.
Shengxi ChenCenter for BioEnergetics, Biodesign Institute, and Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287, United States.
Sidney M HechtCenter for BioEnergetics, Biodesign Institute, and Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287, United States.
BioEnergetics (United States) · USArizona State University · US

Funding

Selection of Modified Ribosomes Using Novel PuromycinsR01GM103861 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI HECHT, SIDNEY M. · 2013 to 2021
$1.6M
NIGMS NIH HHS GM103861NIGMS NIH HHS R01 GM103861
6 · The paper itself

Abstract

In an earlier study, β³-puromycin was used for the selection of modified ribosomes, which were utilized for the incorporation of five different β-amino acids into Escherichia coli dihydrofolate reductase (DHFR). The selected ribosomes were able to incorporate structurally disparate β-amino acids into DHFR, in spite of the use of a single puromycin for the selection of the individual clones. In this study, we examine the extent to which the structure of the β³-puromycin employed for ribosome selection influences the regio- and stereochemical preferences of the modified ribosomes during protein synthesis; the mechanistic probe was a single suppressor tRNA(CUA) activated with each of four methyl-β-alanine isomers (1-4). The modified ribosomes were found to incorporate each of the four isomeric methyl-β-alanines into DHFR but exhibited a preference for incorporation of 3(S)-methyl-β-alanine (β-mAla; 4), i.e., the isomer having the same regio- and stereochemistry as the O-methylated β-tyrosine moiety of β³-puromycin. Also conducted were a selection of clones that are responsive to β²-puromycin and a demonstration of reversal of the regio- and stereochemical preferences of these clones during protein synthesis. These results were incorporated into a structural model of the modified regions of 23S rRNA, which included in silico prediction of a H-bonding network. Finally, it was demonstrated that incorporation of 3(S)-methyl-β-alanine (β-mAla; 4) into a short α-helical region of the nucleic acid binding domain of hnRNP LL significantly stabilized the helix without affecting its DNA binding properties.

Indexed as

Models, MolecularAlanineEscherichia coliEscherichia coli ProteinsHeterogeneous-Nuclear Ribonucleoprotein LHumansHydrogen BondingMolecular Dynamics SimulationMutant ProteinsNucleotide MotifsPeptidyl TransferasesProtein ConformationProtein StabilityPuromycinRecombinant ProteinsRibosomesAlanineEscherichia coli ProteinsFolM protein, E coliHeterogeneous-Nuclear Ribonucleoprotein LMutant ProteinsPeptidyl TransferasesPuromycinRecombinant ProteinsRNA, BacterialRNA, RibosomalRNA, Ribosomal, 23SRNA, Transfer, Amino AcylTetrahydrofolate Dehydrogenase

Identifiers

PMID25982410
PMCPMC4472090
OpenAlexW2291071388

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.