Evidence map›Paper›PMID 23143101›Full record

ArticleNucleic acids research2013

Genetic interactions suggest multiple distinct roles of the arch and core helicase domains of Mtr4 in Rrp6 and exosome function.

A Alejandra Klauer, Ambro van Hoof

Abstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
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  12. Article
  13. Threading the barrel of the RNA exosome.Trends in biochemical sciences · 2013
    Review
  14. 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

2 authors.

A Alejandra KlauerDepartment of Microbiology and Molecular Genetics, University of Texas Health Science Center-Houston and The University of Texas Graduate School of Biomedical Sciences, 6431 Fannin Street, MSB 1.212, Houston, TX 77030, USA.
Ambro van Hoof

Funding

RNA decay and processing activities of the RNA exosomeR01GM099790 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI VAN HOOF, AMBRO · 2012 to 2020
$2.6M
METABOLISM OF YEAST mRNAS THAT LACK A STOP CODONR01GM069900 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI VAN HOOF, AMBRO · 2005 to 2009
$1.4M
NIGMS NIH HHS GM069900NIGMS NIH HHS GM099790NIGMS NIH HHS R01 GM099790
6 · The paper itself

Abstract

The RNA exosome is responsible for a wide variety of RNA processing and degradation reactions. The activity and specificity of the RNA exosome is thought to be controlled by a number of cofactors. Mtr4 is an essential RNA-dependent adenosine triphosphatase that is required for all of the nuclear functions of the RNA exosome. The crystal structure of Mtr4 uncovered a domain that is conserved in the RNA exosome cofactors Mtr4 and Ski2 but not in other helicases, suggesting it has an important role related to exosome activation. Rrp6 provides the nuclear exosome with one of its three nuclease activities, and previous findings suggested that the arch domain is specifically required for Rrp6 functions. Here, we report that the genetic interactions between the arch domain of Mtr4 and Rrp6 cannot be explained by the arch domain solely acting in Rrp6-dependent processing reactions. Specifically, we show that the arch domain is not required for all Rrp6 functions, and that the arch domain also functions independently of Rrp6. Finally, we show that the arch domain of Ski2, the cytoplasmic counterpart of Mtr4, is required for Ski2's function, thereby confirming that the arch domains of these cofactors function independently of Rrp6.

Indexed as

CytoplasmDEAD-box RNA HelicasesDNA-Directed RNA PolymerasesExosome Multienzyme Ribonuclease ComplexGene DeletionProtein Structure, TertiaryRNA Processing, Post-TranscriptionalRNA, Small NucleolarSaccharomyces cerevisiae ProteinsDEAD-box RNA HelicasesDNA-Directed RNA PolymerasesExosome Multienzyme Ribonuclease ComplexMTR4 protein, S cerevisiaeRNA, Small NucleolarRRP6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSKI2 protein, S cerevisiaeTrf5 protein, S cerevisiae

Identifiers

PMID23143101
PMCPMC3592479

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Registered trials

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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.