Evidence map›Paper›PMID 31114923›Full record

ArticleNucleic acids research2019

Conformational communication mediates the reset step in t6A biosynthesis.

Amit Luthra, Naduni Paranagama, William Swinehart, Susan Bayooz, Phuc Phan, Vanessa Quach, Jamie M Schiffer, Boguslaw Stec, Dirk Iwata-Reuyl, Manal A Swairjo

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. 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
1.4field-weighted citation impact, top 19% 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

20 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Catalytic and regulatory basis of tRNA tNature communications · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  8. Article
  9. Conservation and Diversification of tRNA tInternational journal of molecular sciences · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Metal utilization in genome-reduced bacteria: Do human mycoplasmas rely on iron?Computational and structural biotechnology journal · 2021
    Review
  16. Article
  17. Article
  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

10 authors at 3 institutions in 1 country.

Amit LuthraDepartment of Chemistry and Biochemistry, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182, USA.
Naduni ParanagamaDepartment of Chemistry and Biochemistry, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182, USA.
William SwinehartDepartment of Chemistry, Portland State University, PO Box 751, Portland, OR 97207, USA.
Susan BayoozDepartment of Chemistry and Biochemistry, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182, USA.
Phuc PhanDepartment of Chemistry and Biochemistry, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182, USA.
Vanessa QuachDepartment of Chemistry and Biochemistry, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182, USA.
Jamie M SchifferSchrödinger, 10201 Wateridge Cir Suite 220, San Diego, CA 92121, USA.
Boguslaw StecDepartment of Chemistry and Biochemistry, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182, USA.
Dirk Iwata-ReuylDepartment of Chemistry, Portland State University, PO Box 751, Portland, OR 97207, USA.
Manal A SwairjoDepartment of Chemistry and Biochemistry, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182, USA.
San Diego State University · USPortland State University · USSchrodinger (United States) · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
RNA modification: Structure and MechanismR01GM110588 · NIGMS · WESTERN UNIVERSITY OF HEALTH SCIENCES · PI SWAIRJO, MANAL A · 2014 to 2024
$3.9M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM110588
6 · The paper itself

Abstract

The universally conserved N6-threonylcarbamoyladenosine (t6A) modification of tRNA is essential for translational fidelity. In bacteria, t6A biosynthesis starts with the TsaC/TsaC2-catalyzed synthesis of the intermediate threonylcarbamoyl adenylate (TC-AMP), followed by transfer of the threonylcarbamoyl (TC) moiety to adenine-37 of tRNA by the TC-transfer complex comprised of TsaB, TsaD and TsaE subunits and possessing an ATPase activity required for multi-turnover of the t6A cycle. We report a 2.5-Å crystal structure of the T. maritima TC-transfer complex (TmTsaB2D2E2) bound to Mg2+-ATP in the ATPase site, and substrate analog carboxy-AMP in the TC-transfer site. Site directed mutagenesis results show that residues in the conserved Switch I and Switch II motifs of TsaE mediate the ATP hydrolysis-driven reactivation/reset step of the t6A cycle. Further, SAXS analysis of the TmTsaB2D2-tRNA complex in solution reveals bound tRNA lodged in the TsaE binding cavity, confirming our previous biochemical data. Based on the crystal structure and molecular docking of TC-AMP and adenine-37 in the TC-transfer site, we propose a model for the mechanism of TC transfer by this universal biosynthetic system.

Indexed as

AdenosineAdenosine TriphosphatasesAmino Acid MotifsBacterial ProteinsModels, MolecularMutagenesisProtein ConformationRNA, TransferThermotoga maritimaAdenosineAdenosine TriphosphatasesBacterial ProteinsN(6)-(N-threonylcarbonyl)adenosineRNA, Transfer

Identifiers

PMID31114923
PMCPMC6614819
OpenAlexW2946423216

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.