Evidence map›Paper›PMID 21712243›Full record

ArticleNucleic acids research2011

Diauxic shift-dependent relocalization of decapping activators Dhh1 and Pat1 to polysomal complexes.

Sheona P Drummond, John Hildyard, Helena Firczuk, Onrapak Reamtong, Ning Li, Shichina Kannambath, Amy J Claydon, Robert J Beynon, Claire E Eyers, John E G McCarthy

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

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  5. Translational repression of theRNA (New York, N.Y.) · 2017
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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

10 authors at 1 institution in 1 country.

Sheona P DrummondManchester Interdisciplinary Biocentre, University of Manchester, Manchester, UK.
John Hildyard
Helena Firczuk
Onrapak Reamtong
Ning Li
Shichina Kannambath
Amy J Claydon
Robert J Beynon
Claire E Eyers
John E G McCarthy
University of Liverpool · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E003192/1Biotechnology and Biological Sciences Research Council BB/E015778Biotechnology and Biological Sciences Research Council BB/E015778/1Biotechnology and Biological Sciences Research Council BB/E024181/1Biotechnology and Biological Sciences Research Council BB/F019483/1Biotechnology and Biological Sciences Research Council BB/F019963/1Biotechnology and Biological Sciences Research Council BBF019963/1
6 · The paper itself

Abstract

Dhh1 and Pat1 in yeast are mRNA decapping activators/translational repressors thought to play key roles in the transition of mRNAs from translation to degradation. However, little is known about the physical and functional relationships between these proteins and the translation machinery. We describe a previously unknown type of diauxic shift-dependent modulation of the intracellular locations of Dhh1 and Pat1. Like the formation of P bodies, this phenomenon changes the spatial relationship between components involved in translation and mRNA degradation. We report significant spatial separation of Dhh1 and Pat1 from ribosomes in exponentially growing cells. Moreover, biochemical analyses reveal that these proteins are excluded from polysomal complexes in exponentially growing cells, indicating that they may not be associated with active states of the translation machinery. In contrast, under diauxic growth shift conditions, Dhh1 and Pat1 are found to co-localize with polysomal complexes. This work suggests that Dhh1 and Pat1 functions are modulated by a re-localization mechanism that involves eIF4A. Pull-down experiments reveal that the intracellular binding partners of Dhh1 and Pat1 change as cells undergo the diauxic growth shift. This reveals a new dimension to the relationship between translation activity and interactions between mRNA, the translation machinery and decapping activator proteins.

Indexed as

Protein BiosynthesisDEAD-box RNA HelicasesPolyribosomesRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDEAD-box RNA HelicasesDHH1 protein, S cerevisiaePAT1 protein, S cerevisiaeRNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID21712243
PMCPMC3177209
OpenAlexW2157377735

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.