Evidence map›Paper›PMID 10482526›Full record

ArticleJournal of bacteriology1999

The Caulobacter crescentus CgtA protein displays unusual guanine nucleotide binding and exchange properties.

B Lin, K L Covalle, J R Maddock

Abstract 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
–field-weighted citation impact
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.

  1. Article
  2. YbiB: a novel interactor of the GTPase ObgE.Nucleic acids research · 2023
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The universally conserved prokaryotic GTPases.Microbiology and molecular biology reviews : MMBR · 2011
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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

3 authors.

B LinDepartment of Biology, University of Michigan, Ann Arbor, Michigan 48109-1048, USA.
K L Covalle
J R Maddock

Funding

BIOCHEMICAL AND GENETIC ANALYSIS OF CGTA IN CAULOBACTERR01GM055133 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MADDOCK, JANINE R. · 1998 to 2002
$559k
NIGMS NIH HHS GM-55133NIGMS NIH HHS R01 GM055133
6 · The paper itself

Abstract

The Caulobacter crescentus CgtA protein is a member of the Obg-GTP1 subfamily of monomeric GTP-binding proteins. In vitro, CgtA specifically bound GTP and GDP but not GMP or ATP. CgtA bound GTP and GDP with moderate affinity at 30 degrees C and displayed equilibrium binding constants of 1.2 and 0.5 microM, respectively, in the presence of Mg(2+). In the absence of Mg(2+), the affinity of CgtA for GTP and GDP was reduced 59- and 6-fold, respectively. N-Methyl-3'-O-anthranoyl (mant)-guanine nucleotide analogs were used to quantify GDP and GTP exchange. Spontaneous dissociation of both GDP and GTP in the presence of 5 to 12 mM Mg(2+) was extremely rapid (k(d) = 1.4 and 1.5 s(-1), respectively), 10(3)- to 10(5)-fold faster than that of the well-characterized eukaryotic Ras-like GTP-binding proteins. The dissociation rate constant of GDP increased sevenfold in the absence of Mg(2+). Finally, there was a low inherent GTPase activity with a single-turnover rate constant of 5.0 x 10(-4) s(-1) corresponding to a half-life of hydrolysis of 23 min. These data clearly demonstrate that the guanine nucleotide binding and exchange properties of CgtA are different from those of the well-characterized Ras-like GTP-binding proteins. Furthermore, these data are consistent with a model whereby the nucleotide occupancy of CgtA is controlled by the intracellular levels of guanine nucleotides.

Indexed as

Bacterial ProteinsMonomeric GTP-Binding ProteinsCaulobacter crescentusCloning, MolecularGTP-Binding ProteinsGuanosine DiphosphateGuanosine TriphosphateKineticsMagnesiumPolymerase Chain ReactionRecombinant ProteinsBacterial ProteinsCgtA protein, bacteriaGTP-Binding ProteinsGuanosine DiphosphateGuanosine TriphosphateMagnesiumMonomeric GTP-Binding ProteinsRecombinant Proteins

Identifiers

PMID10482526
PMCPMC94105

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.