Evidence map›Paper›PMID 10322018›Full record

ArticleJournal of bacteriology1999

Enhanced function conferred on low-abundance chemoreceptor Trg by a methyltransferase-docking site.

X Feng, A A Lilly, G L Hazelbauer

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
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  7. Paradoxical enhancement of chemoreceptor detection sensitivity by a sensory adaptation enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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  10. Selective allosteric coupling in core chemotaxis signaling complexes.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
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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

3 authors at 1 institution in 1 country.

X FengDepartment of Biochemistry and Biophysics, Washington State University, Pullman, Washington 99164-4660, USA.
A A Lilly
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 GM 20963NIGMS 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 higher than those of low-abundance receptors. These two classes exhibit inherent differences in functional activity. As sole cellular chemoreceptors, high-abundance receptors are effective in methyl-accepting activity, in establishing a functional balance between the two directions of flagellar rotation, in timely adaptation, and in mediating efficient chemotaxis. Low-abundance receptors are not, even when their cellular content is increased. We found that the low-abundance receptor Trg acquired essential functional features of a high-abundance receptor by the addition of the final 19 residues of the high-abundance receptor Tsr. The carboxy terminus of this addition carried a methyltransferase-binding pentapeptide, NWETF, present in high-abundance receptors but absent in the low-abundance class. Provision of this docking site not only enhanced steady-state and adaptational methylation but also shifted the abnormal, counterclockwise bias of flagellar rotation toward a more normal rotational balance and vastly improved chemotaxis in spatial gradients. These improvements can be understood as the result of both enhanced kinase activation by the more methylated receptor and timely adaptation by more efficient methyl-accepting activity. We conclude that the crucial functional difference between the low-abundance receptor Trg and its high-abundance counterparts is the level of methyl-accepting activity conferred by the methyltransferase-docking site.

Indexed as

Escherichia coli ProteinsAmino Acid SequenceBacterial ProteinsBinding SitesBlotting, WesternChemotaxisEscherichia coliFlagellaMembrane ProteinsMethylationMethyltransferasesMolecular Sequence DataReceptors, Cell SurfaceRecombinant Fusion ProteinsRiboseRotationBacterial ProteinsEscherichia coli ProteinsMembrane ProteinsMethyltransferasesReceptors, Cell SurfaceRecombinant Fusion ProteinsRiboseSerineTrg protein, E coliTsr protein, Bacteria

Identifiers

PMID10322018
PMCPMC93772
OpenAlexW2116890296

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.