Evidence map›Paper›PMID 14744139›Full record

ArticleBiochemistry2004

Discrimination between different methylation states of chemotaxis receptor Tar by receptor methyltransferase CheR.

Eduardo Perez, Ann H West, Ann M Stock, Snezana Djordjevic

Open access · greenAbstract readComparative Study
In one paragraph

Article in Biochemistry, 2004. 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
0.8field-weighted citation impact, top 31% 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, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. 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
  7. Article
  8. Article
  9. Article
  10. Article
  11. Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  12. Article
  13. Article
  14. 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 1 institution in 2 countries.

Eduardo PerezCenter for Advanced Biotechnology and Medicine, Department of Biochemistry, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
Ann H West
Ann M Stock
Snezana Djordjevic
Howard Hughes Medical Institute · US

Funding

Structure and Function of Response Regulator ProteinsR37GM047958 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI STOCK, ANN M. · 2003 to 2013
$3.4M
STRUCTURE/FUNCTION OF RESPONSE REGULATOR PROTEINSR01GM047958 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI STOCK, ANN M. · 1992 to 2017
$2.3M
GRADUATE TRAINING IN CELLULAR AND MOLECULAR BIOLOGYT32GM008360 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI MADURA, KIRAN · 1991 to 2011
$1.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM047958NIGMS NIH HHS R37 GM047958NIGMS NIH HHS T32 GM008360NIGMS NIH HHS T32 GM08360
6 · The paper itself

Abstract

Bacterial chemotaxis receptors are posttranslationally modified by carboxyl methylation of specific glutamate residues within their cytoplasmic domains. This highly regulated, reversible modification counterbalances the signaling effects of ligand binding and contributes to adaptation. On the basis of the crystal structure of the gamma-glutamyl methyltransferase CheR, we have postulated that positively charged residues in helix alpha2 in the N-terminal domain of the enzyme may be complementary to the negatively charged methylation region of the methyltransferase substrates, the bacterial chemotaxis receptors. Several altered CheR proteins, in which positively charged arginine or lysine residues were substituted with alanines, were constructed and assayed for their methylation activities toward wild-type receptor and a series of receptor variants containing different glutamates available for methylation. One of the CheR mutant proteins (Arg53Ala) showed significantly lower activity toward all receptor constructs, suggesting that Arg53 may play a general role in catalysis of methyl transfer. The rest of the mutant proteins exhibited different patterns of relative methylation rates toward different receptor substrates, indicating specificity, probably through interaction of CheR with the receptor at sites distal to the specific site of methylation. The findings imply complementarity between positively charged residues of the alpha2 helix of CheR and the negatively charged glutamates of the receptor. It is likely that this complementarity is involved in discriminating different methylation states of the receptors.

Indexed as

AlanineAmino Acid SequenceAmino Acid SubstitutionArginineBacterial ProteinsBinding SitesCatalysisChemoreceptor CellsEscherichia coli ProteinsMethylationMethyltransferasesMolecular Sequence DataProtein Structure, SecondaryReceptors, Cell SurfaceSalmonella typhimuriumSequence DeletionAlanineArginineBacterial Proteinschemotaxis methyltransferaseEscherichia coli ProteinsMethyltransferasesReceptors, Cell SurfaceTar protein, E coli

Identifiers

PMID14744139
PMCPMC3645282
OpenAlexW1975835778

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.