Evidence map›Paper›PMID 30217865›Full record

ArticleRNA (New York, N.Y.)2018

tRNA 3'-amino-tailing for stable amino acid attachment.

Howard Gamper, Ya-Ming Hou

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  12. Practical Synthesis ofACS chemical biology · 2023
    Article
  13. Review
  14. Article
  15. Article
  16. Synthesis of Stably Charged Arg-tRNAMethods in molecular biology (Clifton, N.J.) · 2023
    Article
  17. Article
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Howard GamperDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
Ya-Ming HouDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.ORCID 0000-0001-6546-2597
Thomas Jefferson University · US

Funding

AdoMet-dependent tRNA methyl transferasesR01GM114343 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2015 to 2018
$1.3M
Probe discovery for tRNA methylationR01GM126210 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING, SMITH, LAYTON HARRIS · 2018 to 2020
$1.2M
Probes for a tRNA modification enzymeU01GM108972 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2015 to 2016
$603k
Probes for a tRNA modification enzymeR01GM108972 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2014 to 2014
$295k
NIGMS NIH HHS R01 GM108972NIGMS NIH HHS R01 GM114343NIGMS NIH HHS R01 GM126210NIGMS NIH HHS U01 GM108972NIH HHS GM108972NIH HHS GM114343NIH HHS GM126210
6 · The paper itself

Abstract

Amino acids are attached to the tRNA 3'-end as a prerequisite for entering the ribosome for protein synthesis. Amino acid attachment also gives tRNA access to nonribosomal cellular activities. However, the normal attachment is via an ester linkage between the carboxylic group of the amino acid and the 3'-hydroxyl of the terminal A76 ribose in tRNA. The instability of this ester linkage has severely hampered studies of aminoacyl-tRNAs. Although the use of 3'-amino-3'-deoxy A76 in a 3'-amino-tailed tRNA provides stable aminoacyl attachment via an amide linkage, there are multiple tailing protocols and the efficiency of each relative to the others is unknown. Here we compare five different tailing protocols in parallel, all dependent on the CCA-adding enzyme [CTP(ATP): tRNA nucleotidyl transferase; abbreviated as the CCA enzyme] to exchange the natural ribose with the modified one. We show that the most efficient protocol is achieved by the CCA-catalyzed pyrophosphorolysis removal of the natural A76 in equilibrium with the addition of the appropriate ATP analog to synthesize the modified 3'-end. This protocol for 3'-amino-tailing affords quantitative and stable attachment of a broad range of amino acids to tRNA, indicating its general utility for studies of aminoacyl-tRNAs in both canonical and noncanonical activities.

Indexed as

Adenosine TriphosphateAmino AcidsAmino Acyl-tRNA SynthetasesBinding SitesCatalysisEscherichia coliProtein BiosynthesisRNA, TransferRNA, Transfer, Amino AcylAdenosine TriphosphateAmino AcidsAmino Acyl-tRNA SynthetasesRNA, TransferRNA, Transfer, Amino Acyl3′-amino-3′-deoxy tRNAaminoacylationaminoacyl-tRNACCA-adding enzymeclass I and class IIprolyl-tRNAstreptavidin-biotin

Identifiers

PMID30217865
PMCPMC6239183
OpenAlexW2891025373

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.