Evidence map›Paper›PMID 25589546›Full record

ArticleNucleic acids research2015

Interaction between the RNA-dependent ATPase and poly(A) polymerase subunits of the TRAMP complex is mediated by short peptides and important for snoRNA processing.

Jillian S Losh, Alejandra Klauer King, Jeremy Bakelar, Lacy Taylor, John Loomis, Jason A Rosenzweig, Sean J Johnson, Ambro van Hoof

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Circulating serum exosomes i-tRF-AspGTC and tRF-1-SerCGA as diagnostic indicators for non-small cell lung cancer.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2024
    Article
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  5. Article
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  7. Article
  8. Article
  9. The multitasking polyA tail: nuclear RNA maturation, degradation and export.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
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  11. Article
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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

8 authors at 4 institutions in 1 country.

Jillian S Losh
Alejandra Klauer King
Jeremy Bakelar
Lacy Taylor
John Loomis
Jason A Rosenzweig
Sean J Johnson
Ambro van Hoof
The University of Texas Health Science Center at Houston · USUtah State University · USTexas Southern University · USUniversity of Houston · US

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
NIGMS NIH HHS R01GM099790
6 · The paper itself

Abstract

The RNA exosome is one of the main 3′ to 5′ exoribonucleases in eukaryotic cells. Although it is responsible for degradation or processing of a wide variety of substrate RNAs, it is very specific and distinguishes between substrate and non-substrate RNAs as well as between substrates that need to be 3′ processed and those that need to be completely degraded. This specificity does not appear to be determined by the exosome itself but rather by about a dozen other proteins. Four of these exosome cofactors have enzymatic activity, namely, the nuclear RNA-dependent ATPase Mtr4, its cytoplasmic paralog Ski2 and the nuclear non-canonical poly(A) polymerases, Trf4 and Trf5. Mtr4 and either Trf4 or Trf5 assemble into a TRAMP complex. However, how these enzymes assemble into a TRAMP complex and the functional consequences of TRAMP complex assembly remain unknown. Here, we identify an important interaction site between Mtr4 and Trf5, and show that disrupting the Mtr4/Trf interaction disrupts specific TRAMP and exosome functions, including snoRNA processing.

Indexed as

Adenosine TriphosphatasesPeptidesPolynucleotide AdenylyltransferaseProtein BindingRNA Processing, Post-TranscriptionalRNA, Small NucleolarSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesAdenosine TriphosphatasesPeptidesPolynucleotide AdenylyltransferaseRNA-dependent ATPaseRNA, Small NucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID25589546
PMCPMC4330371
OpenAlexW2169771721

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.