Evidence map›Paper›PMID 21071662›Full record

ArticleScience (New York, N.Y.)2010

How the CCA-adding enzyme selects adenine over cytosine at position 76 of tRNA.

Baocheng Pan, Yong Xiong, Thomas A Steitz

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Crystal structure of the CCA-adding enzyme fromJournal of structural biology: X · 2025
    Article
  4. Article
  5. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  6. Article
  7. Thomas A. Steitz (1940-2018).RNA (New York, N.Y.) · 2019
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. An inhibitory C-terminal region dictates the specificity of A-adding enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  17. Article
  18. Article
  19. Article
  20. Controlling translation via modulation of tRNA levels.Wiley interdisciplinary reviews. RNA
    Review
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

3 authors.

Baocheng PanDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Yong Xiong
Thomas A Steitz

Funding

STRUCTURES OF DNA POLYMERASES AND FUNCTIONAL COMPLEXESR01GM057510 · NIGMS · YALE UNIVERSITY · PI STEITZ, THOMAS ARTHUR · 1998 to 2013
$4.5M
Howard Hughes Medical InstituteNIGMS NIH HHS GM57510NIGMS NIH HHS R01 GM057510
6 · The paper itself

Abstract

CCA-adding enzymes [ATP(CTP):tRNA nucleotidyltransferases] add CCA onto the 3' end of transfer RNA (tRNA) precursors without using a nucleic acid template. Although the mechanism by which cytosine (C) is selected at position 75 of tRNA has been established, the mechanism by which adenine (A) is selected at position 76 remains elusive. Here, we report five cocrystal structures of the enzyme complexed with both a tRNA mimic and nucleoside triphosphates under catalytically active conditions. These structures suggest that adenosine 5'-monophosphate is incorporated onto the A76 position of the tRNA via a carboxylate-assisted, one-metal-ion mechanism with aspartate 110 functioning as a general base. The discrimination against incorporation of cytidine 5'-triphosphate (CTP) at position 76 arises from improper placement of the α phosphate of the incoming CTP, which results from the interaction of C with arginine 224 and prevents the nucleophilic attack by the 3' hydroxyl group of cytidine75.

Indexed as

AdenineAdenosine MonophosphateAdenosine TriphosphateArchaeoglobus fulgidusCatalytic DomainCrystallizationCrystallography, X-RayCytidine TriphosphateCytosineHydrogen BondingModels, MolecularNucleic Acid ConformationProtein ConformationProtein Structure, TertiaryRNA NucleotidyltransferasesRNA, TransferAdenineAdenosine MonophosphateAdenosine TriphosphateCytidine TriphosphateCytosineRNA NucleotidyltransferasesRNA, TransfertRNA nucleotidyltransferase

Identifiers

PMID21071662
PMCPMC3087442

What OpenQuestion holds

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Registered trials

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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.