Evidence map›Paper›PMID 16621838›Full record

ArticleJournal of bacteriology2006

Functional characterization of Escherichia coli GlpG and additional rhomboid proteins using an aarA mutant of Providencia stuartii.

Katy M Clemmer, Gwen M Sturgill, Alexander Veenstra, Philip N Rather

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2006. 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
1.9field-weighted citation impact, top 14% 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, 34 citations in OpenAlex.

  1. Article
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  13. Rhomboid protease dynamics and lipid interactions.Structure (London, England : 1993) · 2009
    Article
  14. Article
  15. Review
  16. Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by activating TatA of the twin-arginine translocase.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  17. Structural basis for intramembrane proteolysis by rhomboid serine proteases.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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 4 institutions in 1 country.

Katy M ClemmerLaboratories of Microbial Pathogenesis, Atlanta VA Medical Center, Atlanta, Georgia, USA.
Gwen M Sturgill
Alexander Veenstra
Philip N Rather
Atlanta VA Medical Center · USCase Western Reserve University · USEmory University · USUniversity School · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Providencia stuartii AarA protein is a member of the rhomboid family of intramembrane serine proteases and required for the production of an extracellular signaling molecule that regulates cellular functions including peptidoglycan acetylation, methionine transport, and cysteine biosynthesis. Additional aarA-dependent phenotypes include (i) loss of an extracellular yellow pigment, (ii) inability to grow on MacConkey agar, and (iii) abnormal cell division. Since these phenotypes are easily assayed, the P. stuartii aarA mutant serves as a useful host system to investigate rhomboid function. The Escherichia coli GlpG protein was shown to be functionally similar to AarA and rescued the above aarA-dependent phenotypes in P. stuartii. GlpG proteins containing single alanine substitutions at the highly conserved catalytic triad of asparagine (N154A), serine (S201A), or histidine (H254A) residues were nonfunctional. The P. stuartii aarA mutant was also used as a biosensor to demonstrate that proteins from a variety of diverse sources exhibited rhomboid activity. In an effort to further investigate the role of a rhomboid protein in cell physiology, a glpG mutant of E. coli was constructed. In phenotype microarray experiments, the glpG mutant exhibited a slight increase in resistance to the beta-lactam antibiotic cefotaxime.

Indexed as

AgarAnti-Bacterial AgentsBacterial ProteinsBiosensing TechniquesCefotaximeCell DivisionDNA-Binding ProteinsDrug ResistanceEndopeptidasesEscherichia coli ProteinsMembrane ProteinsMutationPigments, BiologicalProvidenciaRecombination, GeneticRepressor ProteinsaarA protein, Providencia stuartiiAgarAnti-Bacterial AgentsBacterial ProteinsCefotaximeDNA-Binding ProteinsEndopeptidasesEscherichia coli ProteinsGlpG protein, E coliMembrane ProteinsPigments, BiologicalRepressor ProteinsSerine Endopeptidases

Identifiers

PMID16621838
PMCPMC1447467
OpenAlexW2029454417

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.