Evidence map›Paper›PMID 18539736›Full record

ArticleJournal of bacteriology2008

The Bradyrhizobium japonicum Irr protein is a transcriptional repressor with high-affinity DNA-binding activity.

Indu Sangwan, Sandra K Small, Mark R O'Brian

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.1field-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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Ironing Out the Unconventional Mechanisms of Iron Acquisition and Gene Regulation inFrontiers in cellular and infection microbiology · 2017
    Review
  6. A bacterial iron exporter for maintenance of iron homeostasis.The Journal of biological chemistry · 2014
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Control of bacterial iron homeostasis by manganese.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Heme-dependent metalloregulation by the iron response regulator (Irr) protein in Rhizobium and other Alpha-proteobacteria.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2009
    Article
  19. 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.

Indu SangwanDepartment of Biochemistry, 140 Farber Hall, State University of New York at Buffalo, Buffalo, New York 14214, USA.
Sandra K Small
Mark R O'Brian
University at Buffalo, State University of New York · US

Funding

Regulation of Bacterial Heme MetabolismR01GM067966 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI O'BRIAN, MARK R · 2004 to 2012
$2.2M
NIGMS NIH HHS R01 GM067966
6 · The paper itself

Abstract

The Irr protein is a global regulator of iron homeostasis in Bradyrhizobium japonicum, and a subset of genes within the Irr regulon are negatively controlled under iron limitation. However, repressor function, high-affinity DNA binding in vitro, or promoter occupancy in vivo of Irr for a negatively regulated gene has not been demonstrated. Here, we show that the blr7895 and bll6680 genes are negatively regulated by Irr as determined by derepression of transcript levels in iron-limited cells of an irr mutant strain. Electrophoretic gel mobility shift analysis showed that a component in extracts of wild-type cells grown under iron limitation bound the iron control elements (ICE) within the promoters of blr7895 and bll6680 identified previously (G. Rudolph, G. Semini, F. Hauser, A. Lindemann, M. Friberg, H. Hennecke, and H. M. Fischer, J. Bacteriol. 188:733-744, 2006). Binding was not observed with extracts of cells from the parent strain grown under high iron conditions or with those from an irr mutant. Furthermore, gel mobility supershift experiments identified Irr as a component of the binding complex. Purified recombinant Irr bound to ICE DNA with high affinity in the presence of divalent metal, with K(d) values of 7 to 19 nM, consistent with a physiological role for Irr as a transcriptional regulator. In addition, in vitro transcription initiated from the blr7895 promoter was inhibited by Irr. Whole-cell cross-linking and immunoprecipitation experiments showed that Irr occupies the promoters of blr7895 and bll6680 in vivo in an iron-dependent manner. The findings demonstrate that Irr is a transcriptional repressor that binds DNA with high affinity.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsBradyrhizobiumCations, DivalentChromatin ImmunoprecipitationDNA, BacterialDNA-Binding ProteinsElectrophoretic Mobility Shift AssayGene DeletionMetalsPromoter Regions, GeneticProtein BindingTranscription FactorsTranscription, GeneticBacterial ProteinsCations, DivalentDNA, BacterialDNA-Binding Proteinsiron response regulator protein, BacteriaMetalsTranscription Factors

Identifiers

PMID18539736
PMCPMC2493276
OpenAlexW2075206000

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.