Evidence map›Paper›PMID 29377792›Full record

ArticleeLife2018

Hsp70-associated chaperones have a critical role in buffering protein production costs.

Zoltán Farkas, Dorottya Kalapis, Zoltán Bódi, Béla Szamecz, Andreea Daraba, Karola Almási, Károly Kovács, Gábor Boross, Ferenc Pál, Péter Horváth and 8 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
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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

18 authors at 2 institutions in 1 country.

Zoltán Farkas *Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.ORCID 0000-0002-5085-3306
Dorottya Kalapis *Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Zoltán BódiSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Béla SzameczSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Andreea DarabaSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Karola AlmásiSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Károly KovácsSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Gábor BorossSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Ferenc PálSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Péter HorváthSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Tamás BalassaSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Csaba MolnárSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Aladár Pettkó-SzandtnerInstitute of Plant Biology, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Éva KlementLaboratory of Proteomic Research, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Edit RutkaiDivision for Biotechnology, Bay Zoltán Nonprofit Ltd, Budapest, Hungary.
Attila SzvetnikDivision for Biotechnology, Bay Zoltán Nonprofit Ltd, Budapest, Hungary.
Balázs PappSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Csaba PálSynthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.ORCID 0000-0002-5187-9903
HUN-REN Szegedi Biológiai Kutatóközpont · HUBay Zoltán Foundation for Applied Research · HU

Funding

European Research Council 648364European Research Council 648364 H2020-ERC-2014-CoGGazdaságfejlesztési és Innovációs Operatív Program GINOP-2.3.2-15-2016-00001Gazdaságfejlesztési és Innovációs Operatív Program GINOP-2.3.2-15-2016-00006Gazdaságfejlesztési és Innovációs Operatív Program GINOP-2.3.2-15-2016-00014Gazdaságfejlesztési és Innovációs Operatív Program GINOP-2.3.2-15-2016-00020Gazdaságfejlesztési és Innovációs Operatív Program GINOP-2.3.2-15-2016-00026Gazdaságfejlesztési és Innovációs Operatív Program GINOP-2.3.2-15-2016-00032Magyar Tudományos Akadémia Bolyai Research ScholarshipMagyar Tudományos Akadémia Lendület Programme LP 2009-013/2012Magyar Tudományos Akadémia Lendület Programme LP 2012-32/2016Magyar Tudományos Akadémia Postdoctoral Fellowship Programme PD-038/2015Magyar Tudományos Akadémia Postdoctoral Fellowship Programme Postdoc2014-85Seventh Framework Programme Initial Training Network METAFLUX 264780Wellcome WT 084314/Z/07/ZWellcome WT 098016/Z/11/ZWellcome Trust 084314
6 · The paper itself

Abstract

Proteins are necessary for cellular growth. Concurrently, however, protein production has high energetic demands associated with transcription and translation. Here, we propose that activity of molecular chaperones shape protein burden, that is the fitness costs associated with expression of unneeded proteins. To test this hypothesis, we performed a genome-wide genetic interaction screen in baker's yeast. Impairment of transcription, translation, and protein folding rendered cells hypersensitive to protein burden. Specifically, deletion of specific regulators of the Hsp70-associated chaperone network increased protein burden. In agreement with expectation, temperature stress, increased mistranslation and a chemical misfolding agent all substantially enhanced protein burden. Finally, unneeded protein perturbed interactions between key components of the Hsp70-Hsp90 network involved in folding of native proteins. We conclude that specific chaperones contribute to protein burden. Our work indicates that by minimizing the damaging impact of gratuitous protein overproduction, chaperones enable tolerance to massive changes in genomic expression.

Indexed as

Energy MetabolismHSP72 Heat-Shock ProteinsMolecular ChaperonesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHSP72 Heat-Shock ProteinsMolecular ChaperonesSaccharomyces cerevisiae Proteinschaperone overloadcomputational biologyevolutionary biologygenetic interactiongenomicsprotein burdenS. cerevisiaesystems biology

Identifiers

PMID29377792
PMCPMC5788500
OpenAlexW2786674626

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.