Evidence map›Paper›PMID 17928292›Full record

ArticleThe Journal of biological chemistry2007

An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli.

Aixin Yan, Ziqiang Guan, Christian R H Raetz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
3.3field-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

94 citing papers in PubMed, 162 citations in OpenAlex.

  1. Article
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  13. Antibacterial Activities of Phenolic Compounds inAntibiotics (Basel, Switzerland) · 2024
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  14. Three-component systems represent a common pathway for extracytoplasmic addition of pentofuranose sugars into bacterial glycans.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Development of aFrontiers in microbiology · 2024
    Article
  17. Article
  18. Article
  19. Review
  20. Article

34 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Aixin YanDepartment of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.
Ziqiang Guan
Christian R H Raetz
Duke University · USDuke Medical Center · US

Funding

STEROL LIPIDSU54GM069338 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 2003 to 2013
$72.2M
BIOSYNTHESIS AND FUNCTION OF LIPOPOLYSACCHARIDESR01GM051310 · NIGMS · DUKE UNIVERSITY · PI ZHOU, PEI · 1994 to 2013
$8.1M
NIGMS NIH HHS GM-069338NIGMS NIH HHS GM-51310NIGMS NIH HHS R01 GM051310NIGMS NIH HHS U54 GM069338
6 · The paper itself

Abstract

Modification of lipid A with the 4-amino-4-deoxy-L-arabinose (L-Ara4N) moiety is required for resistance to polymyxin and cationic antimicrobial peptides in Escherichia coli and Salmonella typhimurium. An operon of seven genes (designated pmrHFIJKLM in S. typhimurium), which is regulated by the PmrA transcription factor and is also present in E. coli, is necessary for the maintenance of polymyxin resistance. We previously elucidated the roles of pmrHFIJK in the biosynthesis and attachment of L-Ara4N to lipid A and renamed these genes arn-BCADT, respectively. We now propose functions for the last two genes of the operon, pmrL and pmrM. Chromosomal inactivation of each of these genes in an E. coli pmrA(c) parent switched its phenotype from polymyxin-resistant to polymyxin-sensitive. Lipid A was no longer modified with L-Ara4N, even though the levels of the lipid-linked donor of the L-Ara4N moiety, undecaprenyl phosphate-alpha-L-Ara4N, were not reduced in the mutants. However, the undecaprenyl phosphate-alpha-L-Ara4N present in the mutants was less concentrated on the periplasmic surface of the inner membrane, as judged by 4-5-fold reduced labeling with the inner membrane-impermeable amine reagent N-hydroxysulfosuccin-imidobiotin. In an arnT mutant of the same pmrA(c) parent, which lacks the enzyme that transfers the L-Ara4N unit to lipid A but retains the same high levels of undecaprenyl phosphate-alpha-L-Ara4N as the parent, N-hydroxysulfosuccinimidobiotin labeling was not reduced. These results implicate pmrL and pmrM, but not arnT, in transporting undecaprenyl phosphate-alpha-L-Ara4N across the inner membrane. PmrM and PmrL, now renamed ArnE and ArnF because of their involvement in L-Ara4N modification of lipid A, may be subunits of an undecaprenyl phosphate-alpha-L-Ara4N flippase.

Indexed as

Amino SugarsAnti-Bacterial AgentsBacterial ProteinsBiological TransportCarboxy-LyasesCarrier ProteinsCell MembraneDrug Resistance, BacterialEscherichia coliGene SilencingHexosyltransferasesLipid AOperonPeriplasmPolymyxinsSalmonella typhimurium4-amino-4-deoxyarabinoseAmino SugarsAnti-Bacterial AgentsBacterial ProteinsCarboxy-LyasesCarrier ProteinsHexosyltransferasesL-Ara4N transferaseLipid ApmrA protein, BacteriaPolymyxinsUDPglucuronate decarboxylase

Identifiers

PMID17928292
PMCPMC2613183
OpenAlexW2092282650

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.