Evidence map›Paper›PMID 9852019›Full record

ArticleJournal of bacteriology1998

Comparison in vitro of a high- and a low-abundance chemoreceptor of Escherichia coli: similar kinase activation but different methyl-accepting activities.

A N Barnakov, L A Barnakova, G L Hazelbauer

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.8field-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

29 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Blue Light Is a Universal Signal forJournal of bacteriology · 2019
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Selective allosteric coupling in core chemotaxis signaling complexes.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Article
  9. Article
  10. Core unit of chemotaxis signaling complexes.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Diversity in chemotaxis mechanisms among the bacteria and archaea.Microbiology and molecular biology reviews : MMBR · 2004
    Review
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 1 institution in 1 country.

A N BarnakovDepartment of Biochemistry and Biophysics, Washington State University, Pullman, Washington 99164-4660, USA.
L A Barnakova
G L Hazelbauer
Washington State University · US

Funding

Molecular Studies of Chemoreception: Administrative Supplement for EquipmentR37GM029963 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI HAZELBAUER, GERALD L. · 2012 to 2021
$5.7M
MOLECULAR STUDIES OF CHEMORECEPTIONR01GM029963 · NIGMS · WASHINGTON STATE UNIVERSITY · PI HAZELBAUER, GERALD L. · 1985 to 2010
$4.2M
NIGMS NIH HHS GM29963NIGMS NIH HHS R01 GM029963NIGMS NIH HHS R37 GM029963
6 · The paper itself

Abstract

In Escherichia coli, high-abundance chemoreceptors are present in cellular amounts approximately 10-fold greater than low-abundance chemoreceptors. Cells containing only low-abundance receptors exhibit abnormally low tumble frequencies and do not migrate effectively in spatial gradients. These defects reflect an inherent activity difference between the two receptor classes. We used in vitro assays to investigate this difference. The low-abundance receptor Trg mediated an approximately 100-fold activation of the kinase CheA, only twofold less than activation by the high-abundance receptor Tar. In contrast, Trg was less than 1/20 as active as Tar for in vitro methylation. As observed for high-abundance receptors, kinase activation by Trg varied with the extend of modification at methyl-accepting sites; low methylation corresponded to low kinase activation. Thus, in Trg-only cells, low receptor methylation would result in low kinase activation, correspondingly low content of phospho-CheY, and a decreased dynamic range over which attractant binding could modulate kinase activity. These features could account for the low tumble frequency and inefficient taxis exhibited by Trg-only cells. Thus, the crucial functional difference between the receptor classes is likely to be methyl-accepting activity. We investigated the structural basis for this functional difference by introducing onto the carboxy terminus of Trg a CheR-binding pentapeptide, usually found only at the carboxy termini of high-abundance receptors. This addition enhanced the in vitro methyl-accepting activity of Trg 10-fold.

Indexed as

Escherichia coli ProteinsBacterial ProteinsChemoreceptor CellsEnzyme ActivationEscherichia coliHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMethylationProtein KinasesReceptors, Cell SurfaceS-AdenosylmethionineBacterial ProteinscheA protein, E colicheY protein, E coliEscherichia coli ProteinsHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsProtein KinasesReceptors, Cell SurfaceS-AdenosylmethionineTar protein, E coliTrg protein, E coli

Identifiers

PMID9852019
PMCPMC107778
OpenAlexW2128747388

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.