Evidence map›Paper›PMID 15489420›Full record

ArticleJournal of bacteriology2004

Rgg regulates growth phase-dependent expression of proteins associated with secondary metabolism and stress in Streptococcus pyogenes.

Michelle A Chaussee, Eduardo A Callegari, Michael S Chaussee

Abstract read
In one paragraph

Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

43 citing papers in PubMed, 73 citations in OpenAlex.

  1. Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  2. Article
  3. Pharmaceutics · 2022
    Article
  4. Pathogens (Basel, Switzerland) · 2021
    Review
  5. TheJournal of bacteriology · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Quorum sensing in group A Streptococcus.Frontiers in cellular and infection microbiology · 2014
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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 at 1 institution in 1 country.

Michelle A ChausseeDivision of Basic Biomedical Sciences, University of South Dakota College of Medicine, Lee Medical Building, 414 East Clark Street, Vermillion, SD 57069-2390, USA. mchausse@usd.edu
Eduardo A Callegari
Michael S Chaussee
University of South Dakota · US

Funding

WESTCORE DNA SEQUENCING AND GENOTYPING CORE FACILITYP20RR016479 · NCRR · UNIVERSITY OF SOUTH DAKOTA · PI EICHLER, BARRETT · 2001 to 2011
$32.2M
Regulation of Streptococcus pyogenes exoproteinsR01AI052147 · NIAID · UNIVERSITY OF SOUTH DAKOTA · PI CHAUSSEE, MICHAEL S · 2004 to 2007
$889k
NCRR NIH HHS P20 RR016479NCRR NIH HHS P20 RR 16479-02NIAID NIH HHS R01 AI052147NIAID NIH HHS R01 AI052147-01A2PHS HHS R01 401507
6 · The paper itself

Abstract

The transcriptional regulatory protein Rgg coordinates amino acid catabolism and virulence factor expression in Streptococcus pyogenes. We used a proteomic approach to compare cytoplasmic proteins isolated from S. pyogenes wild-type strain NZ131 (serotype M49) to proteins isolated from an rgg mutant strain during the exponential and stationary phases of growth. Proteins were separated by two-dimensional gel electrophoresis, and 125 protein spots of interest were identified by tandem mass spectrometry. Comparative analysis of proteins isolated from the isogenic strains revealed that growth phase-associated regulation of enzymes involved in the metabolism of arginine (ArcABC), histidine (HutI), and serine (SdhA) was abrogated in the rgg mutant strain, which synthesized the proteins in the exponential phase of growth. In contrast, the enzymes were detected only among wild-type proteins isolated from organisms in the stationary phase of growth. The differences in protein composition were correlated with previously described metabolic changes. In addition, proteins associated with thermal and oxidative stress responses, including ClpE and ClpL, were present in samples isolated from the rgg mutant strain but not in samples isolated from the wild-type strain. The rgg mutant strain was more tolerant to elevated temperature and puromycin than the wild-type strain; however, the mutant was less tolerant to paraquat. We concluded that Rgg is a global regulatory factor that contributes to growth phase-dependent synthesis of proteins associated with secondary metabolism and oxidative and thermal stress responses.

Indexed as

Gene Expression Regulation, BacterialHeat-Shock ResponseProteomeAmino AcidsBacterial ProteinsDNA-Binding ProteinsHot TemperatureMass SpectrometryMutationOxidative StressStreptococcus pyogenesTrans-ActivatorsAmino AcidsBacterial ProteinsDNA-Binding ProteinsProteomergg protein, StreptococcusTrans-Activators

Identifiers

PMID15489420
PMCPMC523193
OpenAlexW2165698978

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.