Evidence map›Paper›PMID 10735864›Full record

ArticleJournal of bacteriology2000

A study of AroP-PheP chimeric proteins and identification of a residue involved in tryptophan transport.

A J Cosgriff, G Brasier, J Pi, C Dogovski, J P Sarsero, A J Pittard

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 28 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

A J CosgriffDepartment of Microbiology and Immunology, The University of Melbourne, Parkville, Victoria, 3052, Australia.
G Brasier
J Pi
C Dogovski
J P Sarsero
A J Pittard
University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In vivo recombination has been used to make a series of AroP-PheP chimeric proteins. Analysis of their respective substrate profiles and activities has identified a small region within span III of AroP which can confer on a predominantly PheP protein the ability to transport tryptophan. Site-directed mutagenesis of the AroP-PheP chimera, PheP, and AroP has established that a key residue involved in tryptophan transport is tyrosine at position 103 in AroP. Phenylalanine is the residue at the corresponding position in PheP. The use of PheP-specific antisera has shown that the inability of certain chimeras to transport any of the aromatic amino acids is not a result of instability or a failure to be inserted into the membrane. Site-directed mutagenesis has identified two significant AroP-specific residues, alanine 107 and valine 114, which are the direct cause of loss of transport activity in chimeras such as A152P. These residues replace a glycine and an alanine in PheP and flank a highly conserved glutamate at position 110. Some suggestions are made as to the possible functions of these residues in the tertiary structure of the proteins.

Indexed as

Amino Acid Transport SystemsAmino Acid Transport Systems, NeutralEscherichia coli ProteinsAlkaline PhosphataseBacterial ProteinsBase SequenceBinding SitesBiological TransportCarrier ProteinsEscherichia coliGenes, BacterialMembrane Transport ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPromoter Regions, GeneticAlkaline PhosphataseAmino Acid Transport SystemsAmino Acid Transport Systems, NeutralAroP protein, E coliBacterial ProteinsCarrier ProteinsEscherichia coli ProteinsMembrane Transport Proteinsphenylalanine-specific permease, E coliRecombinant Fusion ProteinsTryptophanTyrosine

Identifiers

PMID10735864
PMCPMC111270
OpenAlexW2042058258

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.