Evidence map›Paper›PMID 20870768›Full record

ArticleJournal of bacteriology2011

Mutational analysis of the transmembrane helix 2-HAMP domain connection in the Escherichia coli aspartate chemoreceptor tar.

Gus A Wright, Rachel L Crowder, Roger R Draheim, Michael D Manson

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. 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
1.1field-weighted citation impact, top 20% 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, 26 citations in OpenAlex.

  1. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
    Article
  2. Discovery of a New Chemoeffector forACS bio & med chem Au · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Bacterial chemoreceptors and chemoeffectors.Cellular and molecular life sciences : CMLS · 2015
    Review
  12. Article
  13. Article
  14. Article
  15. Transmembrane signaling is anything but rigid.Journal of bacteriology · 2011
    Article
  16. Article
  17. 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 3 institutions in 3 countries.

Gus A WrightDepartment of Biology, Texas A&M University, College Station, Texas 77843-3258, USA.
Rachel L Crowder
Roger R Draheim
Michael D Manson
Texas A&M University · USStockholm University · SEVanderbilt University · US

Funding

Chemistry-Biology Interface Training GrantT32GM065086 · NIGMS · VANDERBILT UNIVERSITY · PI BACHMANN, BRIAN O, SULIKOWSKI, GARY ALLEN · 2002 to 2022
$7.0M
FUNCTION AND EVOLUTION OF PERIPLASMIC CHEMORECEPTORSR01GM039736 · NIGMS · TEXAS A&M UNIVERSITY SYSTEM · PI MANSON, MICHAEL D. · 1988 to 2005
$1.6M
Tuning two-component signaling systems with protein-membrane interationsF32AI075773 · NIAID · STOCKHOLM UNIVERSITY · PI DRAHEIM, ROGER RUSSELL · 2008 to 2009
$82k
NIAID NIH HHS AI075773NIAID NIH HHS F32 AI075773NIGMS NIH HHS GM065086NIGMS NIH HHS GM 39736NIGMS NIH HHS R01 GM039736NIGMS NIH HHS T32 GM065086
6 · The paper itself

Abstract

Transmembrane helix 2 (TM2) of the Tar chemoreceptor undergoes an inward piston-like displacement of 1 to 3 Å upon binding aspartate. This signal is transmitted to the kinase-control module via the HAMP domain. Within Tar, the HAMP domain forms a parallel four-helix bundle consisting of a dimer of two amphipathic helices connected by a flexible linker. In the nuclear magnetic resonance structure of an archaeal HAMP domain, residues corresponding to the MLLT sequence between Arg-214 at the end of TM2 and Pro-219 of Tar are an N-terminal helical extension of AS1. We modified this region to test whether it behaves as a continuous helical connection between TM2 and HAMP. First, one to four Gly residues were inserted between Thr-218 and Pro-219. Second, the MLLT sequence was replaced with one to nine Gly residues. Third, the sequence was shortened or extended with residues compatible with helix formation. Cells expressing receptors in which the MLLT sequence was shortened to MLL or in which the MLLT sequence was replaced by four Gly residues performed good aspartate chemotaxis. Other mutant receptors supported diminished aspartate taxis. Most mutant receptors had biased signal outputs and/or abnormal patterns of adaptive methylation. We interpret these results to indicate that a strong, permanent helical connection between TM2 and the HAMP domain is not necessary for normal transmembrane signaling.

Indexed as

Amino Acid SequenceChemoreceptor CellsEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialModels, MolecularMutationPeptide FragmentsProtein ConformationProtein Structure, TertiaryReceptors, Cell SurfaceEscherichia coli ProteinsPeptide FragmentsReceptors, Cell SurfaceTar protein, E coli

Identifiers

PMID20870768
PMCPMC3019941
OpenAlexW1983032969

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.