Evidence map›Paper›PMID 26483541›Full record

ArticleThe Journal of biological chemistry2015

TatE as a Regular Constituent of Bacterial Twin-arginine Protein Translocases.

Ekaterina Eimer, Julia Fröbel, Anne-Sophie Blümmel, Matthias Müller

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
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  3. Defining Assembly Pathways by Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024
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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

4 authors at 1 institution in 1 country.

Ekaterina EimerFrom the Institute of Biochemistry and Molecular Biology, Faculty of Biology, and.
Julia FröbelFrom the Institute of Biochemistry and Molecular Biology.
Anne-Sophie BlümmelFrom the Institute of Biochemistry and Molecular Biology, Faculty of Biology, and Spemann Graduate School of Biology and Medicine, University of Freiburg, 79104 Freiburg, Germany.
Matthias MüllerFrom the Institute of Biochemistry and Molecular Biology, matthias.mueller@biochemie.uni-freiburg.de.
University of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Twin-arginine translocation (Tat) systems mediate the transmembrane translocation of completely folded proteins that possess a conserved twin-arginine (RR) motif in their signal sequences. Many Tat systems consist of three essential membrane components named TatA, TatB, and TatC. It is not understood why some bacteria, in addition, constitutively express a functional paralog of TatA called TatE. Here we show, in live Escherichia coli cells, that, upon expression of a Tat substrate protein, fluorescently labeled TatE-GFP relocates from a rather uniform distribution in the plasma membrane into a number of discrete clusters. Clustering strictly required an intact RR signal peptide and the presence of the TatABC subunits, suggesting that TatE-GFP associates with functional Tat translocases. In support of this notion, site-specific photo cross-linking revealed interactions of TatE with TatA, TatB, and TatC. The same approach also disclosed a pronounced tendency of TatE and TatA to hetero-oligomerize. Under in vitro conditions, we found that TatE replaces TatA inefficiently. Our collective results are consistent with TatE being a regular constituent of the Tat translocase in E. coli.

Indexed as

Amino Acid MotifsArginineCell MembraneCross-Linking ReagentsEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicGreen Fluorescent ProteinsMembrane Transport ProteinsMicroscopy, FluorescencePlasmidsProtein BindingProtein FoldingProtein Sorting SignalsProtein TransportArginineCross-Linking ReagentsEscherichia coli ProteinsGreen Fluorescent ProteinsMembrane Transport ProteinsProtein Sorting SignalsTatA protein, E coliTatB protein, E coliTatC protein, E coliTatE protein, E coliEscherichia coli (E. coli)membrane transportprotein cross-linkingprotein translocationtransporttwin-arginine translocation

Identifiers

PMID26483541
PMCPMC4705934
OpenAlexW2180157285

What OpenQuestion holds

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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.