Evidence map›Paper›PMID 28303570›Full record

ArticleFEBS letters2017

Aggregation of Mod5 is affected by tRNA binding with implications for tRNA gene-mediated silencing.

David F Read, Thomas J Waller, Eric Tse, Daniel R Southworth, David R Engelke, Philip J Smaldino

Open access · bronzeAbstract readLetter
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. RNA modifying enzymes shape tRNA biogenesis and function.The Journal of biological chemistry · 2024
    Review
  4. How Big Is the Yeast Prion Universe?International journal of molecular sciences · 2023
    Review
  5. Article
  6. An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity.Journal of visualized experiments : JoVE · 2018
    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

6 authors at 2 institutions in 1 country.

David F ReadBiological Chemistry, University of Michigan, Ann Arbor, MI, USA.
Thomas J WallerBiological Chemistry, University of Michigan, Ann Arbor, MI, USA.
Eric TseBiological Chemistry, University of Michigan, Ann Arbor, MI, USA.
Daniel R SouthworthBiological Chemistry, University of Michigan, Ann Arbor, MI, USA.
David R EngelkeBiological Chemistry, University of Michigan, Ann Arbor, MI, USA.
Philip J SmaldinoBiological Chemistry, University of Michigan, Ann Arbor, MI, USA.
Michigan Medicine · USUniversity of Michigan–Ann Arbor · US

Funding

Nuclear Organization of RNA Polymerase III TranscriptionR01GM082875 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ENGELKE, DAVID R · 2008 to 2011
$1.4M
NIGMS NIH HHS R01 GM082875
6 · The paper itself

Abstract

Mod5 is a multifunctional protein that modifies a subset of tRNAs in the cytoplasm and is also required for an RNA-mediated form of transcriptional silencing. Previous in vivo studies have shown that the nuclear silencing function of Mod5 does not require that the causative tRNA gene encode a Mod5 substrate, although Mod5 is still required. However, previous data have not directly tested whether Mod5 can directly bind substrate and nonsubstrate RNAs. We herein demonstrate that Mod5 directly binds to both substrate and nonsubstrate RNAs, including a highly structured, non-tRNA sequence (5S-rRNA), consistent with previous in vivo data. Furthermore, we show that some RNAs drastically change the aggregation behavior of Mod5 with implications for tRNA gene-mediated silencing.

Indexed as

Gene SilencingAlkyl and Aryl TransferasesElectrophoretic Mobility Shift AssayMicroscopy, FluorescenceProtein BindingRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAlkyl and Aryl TransferasesMOD5 protein, S cerevisiaeRNA, TransferSaccharomyces cerevisiae Proteinsamyloid fiberisopentenyl transferaseMod5protein aggregationRNA bindingtRNA modification

Identifiers

PMID28303570
PMCPMC5468478
OpenAlexW2597080728

What OpenQuestion holds

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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.