Evidence map›Paper›PMID 15273322›Full record

ArticleRNA (New York, N.Y.)2004

Functional analysis of mRNA scavenger decapping enzymes.

Shin-Wu Liu, Xinfu Jiao, Hudan Liu, Meigang Gu, Christopher D Lima, Megerditch Kiledjian

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

39 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The eukaryotic translation initiation factor eIF4E elevates steady-state mProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Molecular basis of the selective processing of short mRNA substrates by the DcpS mRNA decapping enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Article
  8. A Benzophenone-Based Photocaging Strategy for the N7 Position of Guanosine.Angewandte Chemie (International ed. in English) · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. mRNAs biotinylated within the 5' cap and protected against decapping: new tools to capture RNA-protein complexes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Article
  13. Article
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  15. Review
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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

6 authors at 2 institutions in 1 country.

Shin-Wu LiuDepartment of Cell Biology and Neuroscience, Rutgers University, Piscataway, NJ 08854, USA.
Xinfu Jiao
Hudan Liu
Meigang Gu
Christopher D Lima
Megerditch Kiledjian
Rutgers, The State University of New Jersey · USKettering University · US

Funding

STRUCTURAL STUDIES OF THE MRNA CAPPING APPARATUSR01GM061906 · NIGMS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI LIMA, CHRISTOPHER D. · 2000 to 2013
$4.8M
RNA/PROTEIN INTERACTIONS REGULATING MRNA STABILITYR01DK051611 · NIDDK · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI KILEDJIAN, MEGERDITCH · 1997 to 2006
$1.8M
NIDDK NIH HHS DK51611NIDDK NIH HHS R01 DK051611NIGMS NIH HHS GM61906NIGMS NIH HHS R01 GM061906
6 · The paper itself

Abstract

Eukaryotic cells primarily utilize exoribonucleases and decapping enzymes to degrade their mRNA. Two major decapping enzymes have been identified. The hDcp2 protein catalyzes hydrolysis of the 5' cap linked to an RNA moiety, whereas the scavenger decapping enzyme, DcpS, functions on a cap structure lacking the RNA moiety. DcpS is a member of the histidine triad (HIT) family of hydrolases and catalyzes the cleavage of m7GpppN. HIT proteins are homodimeric and contain two conserved 100-amino-acid HIT fold domains with independent active sites that are each sufficient to bind and hydrolyze cognate substrates. We carried out a functional characterization of the DcpS enzyme and demonstrate that unlike previously described HIT proteins, DcpS is a modular protein that requires both the core HIT fold at the carboxyl-terminus and sequences at the amino-terminus of the protein for cap binding and hydrolysis. Interestingly, DcpS can efficiently compete for and hydrolyze the cap structure even in the presence of excess eIF4E, implying that DcpS could function to alleviate the accumulation of complexes between eIF4E and cap structure that would otherwise accumulate following mRNA decay. Using immunofluorescence microscopy, we demonstrate that DcpS is predominantly a nuclear protein, with low levels of detected protein in the cytoplasm. Furthermore, analysis of the endogenous hDcp2 protein reveals that in addition to the cytoplasmic foci, it is also present in the nucleus. These data reveal that both decapping enzymes are contained in the nuclear compartment, indicating that they may fulfill a greater function in the nucleus than previously appreciated.

Indexed as

Base PairingBase SequenceCell NucleusCytoplasmElectrophoretic Mobility Shift AssayEndoribonucleasesEukaryotic Initiation Factor-4EHumansMolecular Sequence DataNucleic Acid ConformationRecombinant ProteinsRNA CapsRNA, MessengerDCP2 protein, humanDcpS protein, humanEndoribonucleasesEukaryotic Initiation Factor-4ERecombinant ProteinsRNA CapsRNA, Messenger

Identifiers

PMID15273322
PMCPMC1370627
OpenAlexW2020376695

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.