Evidence map›Paper›PMID 15882424›Full record

ArticleMolecular microbiology2005

Regulation of purine biosynthesis by a eukaryotic-type kinase in Streptococcus agalactiae.

Lakshmi Rajagopal, Anthony Vo, Aurelio Silvestroni, C E Rubens

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
5.4field-weighted citation impact, top 5% 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

52 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Article
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  4. Identification of glyoxalase A in group BInfection and immunity · 2025
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  5. Population structure and gene flux ofMicrobial genomics · 2025
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  6. Identification of Glyoxalase A in Group BbioRxiv : the preprint server for biology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Proteomic response inJournal of oral microbiology · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. A review of HPRT and its emerging role in cancer.Medical oncology (Northwood, London, England) · 2018
    Review
  19. Transcriptome and Proteome of Fish-PathogenicFrontiers in microbiology · 2018
    Article
  20. 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

4 authors at 1 institution in 1 country.

Lakshmi RajagopalDivision of Infectious Disease and Department of Pediatrics, Children's Hospital and Regional Medical Center and University of Washington, Suite 300, Mail Stop CW, 307 Westlake Ave. North, Seattle, WA 98109, USA. lakshmi.rajagopal@seattlechildrens.org
Anthony Vo
Aurelio Silvestroni
C E Rubens
Seattle Children's Hospital · US

Funding

Role of a novel signal transduction pathway in GBSR01AI056073 · NIAID · SEATTLE CHILDREN'S HOSPITAL · PI RUBENS, CRAIG E. · 2003 to 2007
$1.3M
NIAID NIH HHS R01 AI056073
6 · The paper itself

Abstract

Group B streptococci (GBS) are the principal causal agents of human neonatal pneumonia, sepsis and meningitis. We had previously described the existence of a eukaryotic-type serine/threonine kinase (Stk1) and phosphatase (Stp1) in GBS that regulate growth and virulence of the pathogen. Our previous results also demonstrated that these enzymes reversibly phosphorylated an inorganic pyrophosphatase. To understand the role of these eukaryotic-type enzymes on growth of GBS, we assessed the stk1-mutants for auxotrophic requirements. In this report, we describe that in the absence of the kinase (Stk1), GBS are attenuated for de novo purine biosynthesis and are consequently growth arrested. During growth in media lacking purines, the intracellular G nucleotide pools (GTP, GDP and GMP) are significantly reduced in the Stk1-deficient strains, while levels of A nucleotides (ATP, ADP and AMP) are marginally increased when compared with the isogenic wild-type strain. We provide evidence that the reduced pools of G nucleotides result from altered activity of the IMP utilizing enzymes, adenylosuccinate synthetase (PurA) and IMP dehydrogenase (GuaB) in these strains. We also demonstrate that Stk1 and Stp1 reversibly phosphorylate and consequently regulate PurA activity in GBS. Collectively, these data indicate the novel role of eukaryotic-type kinases in regulation of metabolic processes such as purine biosynthesis.

Indexed as

Adenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateAdenylosuccinate SynthaseGenetic Complementation TestGuanosine DiphosphateGuanosine MonophosphateGuanosine TriphosphateIMP DehydrogenaseMutationPhosphorylationPhosphotransferasesPurinesStreptococcus agalactiaeAdenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateAdenylosuccinate SynthaseGuanosine DiphosphateGuanosine MonophosphateGuanosine TriphosphateIMP DehydrogenasePhosphotransferasesPurines

Identifiers

PMID15882424
PMCPMC2366208
OpenAlexW1532273383

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.