Evidence map›Paper›PMID 21507956›Full record

ArticleThe Journal of biological chemistry2011

A single zinc ion is sufficient for an active Trypanosoma brucei tRNA editing deaminase.

Jessica L Spears, Mary Anne T Rubio, Kirk W Gaston, Ewa Wywial, Alexandros Strikoudis, Janusz M Bujnicki, F Nina Papavasiliou, Juan D Alfonzo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Distribution of ADAT-Dependent Codons in the Human Transcriptome.International journal of molecular sciences · 2015
    Article
  10. Article
  11. Review
  12. Article
  13. 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

8 authors at 4 institutions in 2 countries.

Jessica L SpearsDepartment of Microbiology, The Ohio State Center for RNA Biology, Columbus, Ohio 43210, USA.
Mary Anne T Rubio
Kirk W Gaston
Ewa Wywial
Alexandros Strikoudis
Janusz M Bujnicki
F Nina Papavasiliou
Juan D Alfonzo
The Ohio State University · USRockefeller University · USAdam Mickiewicz University in Poznań · PLInternational Institute of Molecular and Cell Biology · PL

Funding

tRNA editing by deamination: Balancing affinity and specifictyR01GM084065 · NIGMS · OHIO STATE UNIVERSITY · PI ALFONZO, JUAN D · 2008 to 2021
$4.0M
NIGMS NIH HHS GM084065NIGMS NIH HHS R01 GM084065
6 · The paper itself

Abstract

Editing of adenosine (A) to inosine (I) at the first anticodon position in tRNA is catalyzed by adenosine deaminases acting on tRNA (ADATs). This essential reaction in bacteria and eukarya permits a single tRNA to decode multiple codons. Bacterial ADATa is a homodimer with two bound essential Zn(2+). The ADATa crystal structure revealed residues important for substrate binding and catalysis; however, such high resolution structural information is not available for eukaryotic tRNA deaminases. Despite significant sequence similarity among deaminases, we continue to uncover unexpected functional differences between Trypanosoma brucei ADAT2/3 (TbADAT2/3) and its bacterial counterpart. Previously, we demonstrated that TbADAT2/3 is unique in catalyzing two different deamination reactions. Here we show by kinetic analyses and inductively coupled plasma emission spectrometry that wild type TbADAT2/3 coordinates two Zn(2+) per heterodimer, but unlike any other tRNA deaminase, mutation of one of the key Zn(2+)-coordinating cysteines in TbADAT2 yields a functional enzyme with a single-bound zinc. These data suggest that, at least, TbADAT3 may play a role in catalysis via direct coordination of the catalytic Zn(2+). These observations raise the possibility of an unusual Zn(2+) coordination interface with important implications for the function and evolution of editing deaminases.

Indexed as

Adenosine DeaminaseCations, DivalentProtozoan ProteinsRNA-Binding ProteinsRNA EditingRNA, ProtozoanRNA, TransferTrypanosoma brucei bruceiZincADARB1 protein, humanAdenosine DeaminaseCations, DivalentProtozoan ProteinsRNA-Binding ProteinsRNA, ProtozoanRNA, TransferZinc

Identifiers

PMID21507956
PMCPMC3121520
OpenAlexW1974649194

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.