Evidence map›Paper›PMID 16677301›Full record

ArticleMolecular microbiology2006

Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery.

Daisuke Shiomi, Masayuki Yoshimoto, Michio Homma, Ikuro Kawagishi

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

51 citing papers in PubMed, 111 citations in OpenAlex.

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  14. ParP prevents dissociation of CheA from chemotactic signaling arrays and tethers them to a polar anchor.Proceedings of the National Academy of Sciences of the United States of America · 2014
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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 2 countries.

Daisuke ShiomiDivision of Biological Science, Graduate School of Science, Nagoya University, Chikusa-Ku, Nagoya, Japan.
Masayuki Yoshimoto
Michio Homma
Ikuro Kawagishi
Nagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Escherichia coli, chemoreceptor clustering at a cell pole seems critical for signal amplification and adaptation. However, little is known about the mechanism of localization itself. Here we examined whether the aspartate chemoreceptor (Tar) is inserted directly into the polar membrane by using its fusion to green fluorescent protein (GFP). After induction of Tar-GFP, fluorescent spots first appeared in lateral membrane regions, and later cell poles became predominantly fluorescent. Unexpectedly, Tar-GFP showed a helical arrangement in lateral regions, which was more apparent when a Tar-GFP derivative with two cysteine residues in the periplasmic domain was cross-linked to form higher oligomers. Moreover, similar distribution was observed even when the cytoplasmic domain of the double cysteine Tar-GFP mutant was replaced by that of the kinase EnvZ, which does not localize to a pole. Observation of GFP-SecE and a translocation-defective MalE-GFP mutant, as well as indirect immunofluorescence microscopy on SecG, suggested that the general protein translocation machinery (Sec) itself is arranged into a helical array, with which Tar is transiently associated. The Sec coil appeared distinct from the MreB coil, an actin-like cytoskeleton. These findings will shed new light on the mechanisms underlying spatial organization of membrane proteins in E. coli.

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsCell MembraneCell PolarityChemoreceptor CellsCytoplasmEscherichia coliEscherichia coli ProteinsGreen Fluorescent ProteinsMembrane ProteinsMultienzyme ComplexesMutationPeriplasmic Binding ProteinsProtein TransportReceptors, Cell SurfaceSEC Translocation ChannelsBacterial Outer Membrane ProteinsBacterial ProteinsenvZ protein, E coliEscherichia coli ProteinsGreen Fluorescent ProteinsMalE protein, E coliMembrane ProteinsMultienzyme ComplexesPeriplasmic Binding ProteinsReceptors, Cell SurfaceSecE protein, E coliSecG protein, E coliSEC Translocation ChannelsTar protein, E coli

Identifiers

PMID16677301
PMCPMC1513513
OpenAlexW2165328945

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.