Evidence map›Paper›PMID 21148555›Full record

ArticleThe Journal of biological chemistry2011

Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli.

Yi-Hsueh Lu, Ziqiang Guan, Jinshi Zhao, Christian R H Raetz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
2.6field-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

58 citing papers in PubMed, 111 citations in OpenAlex.

  1. Review
  2. Article
  3. Essential Role of LapD in the Absence of Cardiolipins.International journal of molecular sciences · 2026
    Article
  4. Biosynthesis of lanosterol inSynthetic and systems biotechnology · 2025
    Article
  5. Review
  6. PgpP is a broadly conserved phosphatase required for phosphatidylglycerol lipid synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Towards Molecular Understanding of the Functional Role of UbiJ-UbiKInternational journal of molecular sciences · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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 2 institutions in 1 country.

Yi-Hsueh LuDepartment of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.
Ziqiang Guan
Jinshi Zhao
Christian R H Raetz
Duke University · USDuke University Hospital · US

Funding

STEROL LIPIDSU54GM069338 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 2003 to 2013
$72.2M
LIPID A MODIFICATION SYSTEMS IN GRAM-NEGATIVE BACTERIAR37GM051796 · NIGMS · DUKE UNIVERSITY · PI RAETZ, CHRISTIAN R · 1999 to 2008
$3.0M
Lipid A Modification Systems in Gram-Negative BacteriaR01GM051796 · NIGMS · DUKE UNIVERSITY · PI ZHOU, PEI · 1995 to 2012
$1.5M
NIGMS NIH HHS GM-069338NIGMS NIH HHS GM-51796NIGMS NIH HHS R01 GM051796NIGMS NIH HHS R37 GM051796NIGMS NIH HHS U54 GM069338
6 · The paper itself

Abstract

The phospholipids of Escherichia coli consist mainly of phosphatidylethanolamine, phosphatidylglycerol (PG), and cardiolipin. PG makes up ∼25% of the cellular phospholipid and is essential for growth in wild-type cells. PG is synthesized on the inner surface of the inner membrane from cytidine diphosphate-diacylglycerol and glycerol 3-phosphate, generating the precursor phosphatidylglycerol-phosphate (PGP). This compound is present at low levels (∼0.1% of the total lipid). Dephosphorylation of PGP to PG is catalyzed by several PGP-phosphatases. The pgpA and pgpB genes, which encode structurally distinct PGP-phosphatases, were identified previously. Double deletion mutants lacking pgpA and pgpB are viable and still make PG, suggesting the presence of additional phosphatase(s). We have identified a third PGP-phosphatase gene (previously annotated as yfhB but renamed pgpC) using an expression cloning strategy. A mutant with deletions in all three phosphatase genes is not viable unless covered by a plasmid expressing either pgpA, pgpB, or pgpC. When the triple mutant is covered with the temperature-sensitive plasmid pMAK705 expressing any one of the three pgp genes, the cells grow at 30 but not 42 °C. As growth slows at 42 °C, PGP accumulates to high levels, and the PG content declines. PgpC orthologs are present in many other bacteria.

Indexed as

CardiolipinsCell MembraneEscherichia coli K12Escherichia coli ProteinsGene DeletionPhosphoric Monoester HydrolasesCardiolipinsEscherichia coli ProteinsPhosphoric Monoester Hydrolases

Identifiers

PMID21148555
PMCPMC3037664
OpenAlexW1964082146

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.