Evidence map›Paper›PMID 19049984›Full record

ArticleThe Journal of biological chemistry2009

Phosphatidic acid and N-acylphosphatidylethanolamine form membrane domains in Escherichia coli mutant lacking cardiolipin and phosphatidylglycerol.

Eugenia Mileykovskaya, Andrea C Ryan, Xi Mo, Chun-Chieh Lin, Khaled I Khalaf, William Dowhan, Teresa A Garrett

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

42 citing papers in PubMed, 82 citations in OpenAlex.

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  12. Biogenesis, transport and remodeling of lysophospholipids in Gram-negative bacteria.Biochimica et biophysica acta. Molecular and cell biology of lipids · 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

7 authors at 2 institutions in 1 country.

Eugenia MileykovskayaDepartment of Biochemistry and Molecular Biology, University of Texas, Medical School, Houston, Texas 77030. Electronic address: Eugenia.Mileykovskaya@uth.tmc.edu.
Andrea C RyanDepartment of Biochemistry, Duke University, Medical Center, Durham, North Carolina 27710.
Xi MoDepartment of Biochemistry and Molecular Biology, University of Texas, Medical School, Houston, Texas 77030.
Chun-Chieh LinDepartment of Biochemistry and Molecular Biology, University of Texas, Medical School, Houston, Texas 77030.
Khaled I KhalafDepartment of Biochemistry and Molecular Biology, University of Texas, Medical School, Houston, Texas 77030.
William DowhanDepartment of Biochemistry and Molecular Biology, University of Texas, Medical School, Houston, Texas 77030. Electronic address: William.Dowhan@uth.tmc.edu.
Teresa A GarrettDepartment of Chemistry, Vassar College, Poughkeepsie, New York 12604. Electronic address: tegarrett@vassar.edu.
Duke University · USVassar College · US

Funding

STEROL LIPIDSU54GM069338 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 2003 to 2013
$72.2M
Structure and Function in Membrane ProteinsR37GM020478 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DOWHAN, WILLIAM · 2005 to 2015
$5.4M
NIGMS NIH HHS GM-069338NIGMS NIH HHS GM R37-20478
6 · The paper itself

Abstract

The pgsA null Escherichia coli strain, UE54, lacks the major anionic phospholipids phosphatidylglycerol and cardiolipin. Despite these alterations the strain exhibits relatively normal cell division. Analysis of the UE54 phospholipids using negativeion electrospray ionization mass spectrometry resulted in identification of a new anionic phospholipid, N-acylphosphatidylethanolamine. Staining with the fluorescent dye 10-N-nonyl acridine orange revealed anionic phospholipid membrane domains at the septal and polar regions. Making UE54 null in minCDE resulted in budding off of minicells from polar domains. Analysis of lipid composition by mass spectrometry revealed that minicells relative to parent cells were significantly enriched in phosphatidic acid and N-acylphosphatidylethanolamine. Thus despite the absence of cardiolipin, which forms membrane domains at the cell pole and division sites in wild-type cells, the mutant cells still maintain polar/septal localization of anionic phospholipids. These three anionic phospholipids share common physical properties that favor polar/septal domain formation. The findings support the proposed role for anionic phospholipids in organizing amphitropic cell division proteins at specific sites on the membrane surface.

Indexed as

MutationCardiolipinsChromatography, LiquidChromatography, Thin LayerEscherichia coliFluorescent DyesGreen Fluorescent ProteinsLiposomesPhosphatidic AcidsPhosphatidylethanolaminesPhosphatidylglycerolsSpectrometry, Mass, Electrospray IonizationCardiolipinsFluorescent DyesGreen Fluorescent ProteinsLiposomesPhosphatidic AcidsphosphatidylethanolaminePhosphatidylethanolaminesPhosphatidylglycerols

Identifiers

PMID19049984
PMCPMC2631977
OpenAlexW2003361199

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.