Evidence map›Paper›PMID 30401812›Full record

ArticleScientific reports2018

A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells.

Güleycan Lutfullahoğlu-Bal, Ayşe Bengisu Seferoğlu, Abdurrahman Keskin, Emel Akdoğan, Cory D Dunn

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

9 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
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  6. The structure and function of P5A-ATPases.Nature communications · 2024
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  7. 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

5 authors at 2 institutions in 3 countries.

Güleycan Lutfullahoğlu-BalInstitute of Biotechnology, Helsinki Institute of Life Science, University of Helsinki, 00014, Helsinki, Finland.
Ayşe Bengisu SeferoğluInstitute of Biotechnology, Helsinki Institute of Life Science, University of Helsinki, 00014, Helsinki, Finland.
Abdurrahman KeskinDepartment of Molecular Biology and Genetics, Koç University, 34450, Sarıyer, İstanbul, Turkey.
Emel AkdoğanDepartment of Molecular Biology and Genetics, Koç University, 34450, Sarıyer, İstanbul, Turkey.
Cory D DunnInstitute of Biotechnology, Helsinki Institute of Life Science, University of Helsinki, 00014, Helsinki, Finland. cory.dunn@helsinki.fi.ORCID http://orcid.org/0000-0003-2393-5944
University of Helsinki · FIKoç University · TR

Funding

European Research Council 637649
6 · The paper itself

Abstract

Prokaryotes can provide new genetic information to eukaryotes by horizontal gene transfer (HGT), and such transfers are likely to have been particularly consequential in the era of eukaryogenesis. Since eukaryotes are highly compartmentalized, it is worthwhile to consider the mechanisms by which newly transferred proteins might reach diverse organellar destinations. Toward this goal, we have focused our attention upon the behavior of bacteria-derived tail anchors (TAs) expressed in the eukaryote Saccharomyces cerevisiae. In this study, we report that a predicted membrane-associated domain of the Escherichia coli YgiM protein is specifically trafficked to peroxisomes in budding yeast, can be found at a pre-peroxisomal compartment (PPC) upon disruption of peroxisomal biogenesis, and can functionally replace an endogenous, peroxisome-directed TA. Furthermore, the YgiM(TA) can localize to peroxisomes in mammalian cells. Since the YgiM(TA) plays no endogenous role in peroxisomal function or assembly, this domain is likely to serve as an excellent tool allowing further illumination of the mechanisms by which TAs can travel to peroxisomes. Moreover, our findings emphasize the ease with which bacteria-derived sequences might target to organelles in eukaryotic cells following HGT, and we discuss the importance of flexible recognition of organelle targeting information during and after eukaryogenesis.

Indexed as

Amino Acid SequenceEscherichia coliEscherichia coli ProteinsGene Transfer, HorizontalHEK293 CellsHumansMixed Function OxygenasesPeroxisomesProtein TransportSaccharomyces cerevisiaeEscherichia coli ProteinsMixed Function OxygenasesYgiN protein, E coli

Identifiers

PMID30401812
PMCPMC6219538
OpenAlexW2953171688

What OpenQuestion holds

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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.