Evidence map›Paper›PMID 12486044›Full record

ArticleJournal of bacteriology2003

Mutational analysis of a conserved signal-transducing element: the HAMP linker of the Escherichia coli nitrate sensor NarX.

J Alex Appleman, Valley Stewart

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

50 citing papers in PubMed, 89 citations in OpenAlex.

  1. An activator of a two-component system controls cell separation and intrinsic drug resistance inProceedings of the National Academy of Sciences of the United States of America · 2026
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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

2 authors at 1 institution in 1 country.

J Alex ApplemanSection of Microbiology, University of California-Davis, One Shields Avenue, Davis, CA 95616-8665, USA. jaappleman@ucdavis.edu
Valley Stewart
University of California, Davis · US

Funding

GENETIC CONTROL OF NITRATE RESPIRATION IN E. COLIR01GM036877 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI STEWART, VALLEY J. · 1986 to 2010
$2.4M
NIGMS NIH HHS GM 36877NIGMS NIH HHS R01 GM036877
6 · The paper itself

Abstract

The HAMP linker, a predicted structural element observed in sensor proteins from all domains of life, is proposed to transmit signals between extracellular sensory input domains and cytoplasmic output domains. HAMP (histidine kinase, adenylyl cyclase, methyl-accepting chemotaxis protein, and phosphatase) linkers are located just inside the cytoplasmic membrane and are projected to form two short amphipathic alpha-helices (AS-1 and AS-2) joined by an unstructured connector. The presumed helices are comprised of hydrophobic residues in heptad repeats, with only three positions exhibiting strong conservation. We generated missense mutations at these three positions and throughout the HAMP linker in the Escherichia coli nitrate sensor kinase NarX and screened the resulting mutants for defective responses to nitrate. Most missense mutations in this region resulted in a constitutive phenotype mimicking the ligand-bound state, and only one residue (a conserved Glu before AS-2) was essential for HAMP linker function. We also scanned the narX HAMP linker with an overlapping set of seven-residue deletions. Deletions in AS-1 and the connector resulted in constitutive phenotypes. Two deletions in AS-2 resulted in a novel reversed response phenotype in which the response to ligand was the opposite of that seen for the narX(+) strain. These observations are consistent with the proposed HAMP linker structure, show that the HAMP linker plays an active role in transmembrane signal transduction, and indicate that the two amphipathic alpha-helices have different roles in signal transduction.

Indexed as

Bacterial ProteinsDNA Mutational AnalysisSignal TransductionAdenylyl CyclasesAmino Acid SequenceCell MembraneConserved SequenceEscherichia coliEscherichia coli ProteinsGene DeletionHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMolecular Sequence DataMutation, MissenseNitratesAdenylyl CyclasesBacterial ProteinsEscherichia coli ProteinsHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsnarX protein, E coliNitratesPhosphoric Monoester HydrolasesProtein Kinases

Identifiers

PMID12486044
PMCPMC141870
OpenAlexW2131122988

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.