Evidence map›Paper›PMID 24710271›Full record

ArticleMolecular and cellular biology2014

Physical and functional interaction between the methyltransferase Bud23 and the essential DEAH-box RNA helicase Ecm16.

Richa Sardana, Jieyi Zhu, Michael Gill, Arlen W Johnson

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 20% 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, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Structural and functional studies of Bud23-Trm112 reveal 18S rRNA N7-G1575 methylation occurs on late 40S precursor ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Richa SardanaDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, USA.
Jieyi ZhuDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, USA.
Michael GillDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, USA.
Arlen W JohnsonDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, USA arlen@austin.utexas.edu.
The University of Texas at Austin · US

Funding

MRNA DEGRADATION AND TRANSLATION CONTROL IN YEASTR01GM053655 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI JOHNSON, ARLEN W · 1995 to 2017
$5.1M
Biogenesis of the Small Ribosomal Subunit in EukaryotesR01GM108823 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI JOHNSON, ARLEN W · 2014 to 2017
$1.2M
NIGMS NIH HHS R01 GM053655NIGMS NIH HHS R01 GM108823NIGMS NIH HHS R01GM108823NIGMS NIH HHS R01GM53655
6 · The paper itself

Abstract

The small ribosomal subunit assembles cotranscriptionally on the nascent primary transcript. Cleavage at site A2 liberates the pre-40S subunit. We previously identified Bud23 as a conserved eukaryotic methyltransferase that is required for efficient cleavage at A2. Here, we report that Bud23 physically and functionally interacts with the DEAH-box RNA helicase Ecm16 (also known as Dhr1). Ecm16 is also required for cleavage at A2. We identified mutations in ECM16 that suppressed the growth and A2 cleavage defects of a bud23Δ mutant. RNA helicases often require protein cofactors to provide substrate specificity. We used yeast (Saccharomyces cerevisiae) two-hybrid analysis to map the binding site of Bud23 on Ecm16. Despite the physical and functional interaction between these factors, mutations that disrupted the interaction, as assayed by two-hybrid analysis, did not display a growth defect. We previously identified mutations in UTP2 and UTP14 that suppressed bud23Δ. We suggest that a network of protein interactions may mask the loss of interaction that we have defined by two-hybrid analysis. A mutation in motif I of Ecm16 that is predicted to impair its ability to hydrolyze ATP led to accumulation of Bud23 in an ∼45S particle containing Ecm16. Thus, Bud23 enters the pre-40S pathway at the time of Ecm16 function.

Indexed as

Amino Acid SequenceCentrifugationDEAD-box RNA HelicasesGenes, DominantGenetic Complementation TestMethyltransferasesModels, MolecularMolecular Sequence DataMutant ProteinsMutationProtein BindingProtein Interaction Domains and MotifsProtein Interaction MappingRibosomesRNA Processing, Post-TranscriptionalRNA, RibosomalBud23 protein, S cerevisiaeDEAD-box RNA HelicasesECM16 protein, S cerevisiaeMethyltransferasesMutant ProteinsRNA, RibosomalSaccharomyces cerevisiae Proteins

Identifiers

PMID24710271
PMCPMC4054285
OpenAlexW2158108128

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.