Evidence map›Paper›PMID 22072719›Full record

ArticleThe Journal of biological chemistry2011

Phosphorylation of PhoP protein plays direct regulatory role in lipid biosynthesis of Mycobacterium tuberculosis.

Rajni Goyal, Arijit Kumar Das, Ranjeet Singh, Pradip K Singh, Suresh Korpole, Dibyendu Sarkar

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

27 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
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  6. Article
  7. eLife · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Metabolic Switching ofJournal of bacteriology · 2020
    Article
  14. Article
  15. PhoPR Positively RegulatesJournal of bacteriology · 2018
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Evolutionary history of tuberculosis shaped by conserved mutations in the PhoPR virulence regulator.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

6 authors at 2 institutions in 1 country.

Rajni GoyalInstitute of Microbial Technology, Council of Scientific and Industrial Research, Sector 39 A, Chandigarh 160036, India.
Arijit Kumar Das
Ranjeet Singh
Pradip K Singh
Suresh Korpole
Dibyendu Sarkar
Council of Scientific and Industrial Research · INInstitute of Microbial Technology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycobacterium tuberculosis PhoP is essential for virulence and intracellular growth of the tubercle bacilli. Genetic evidence suggests that PhoP regulates complex lipid biosynthesis, and absence of some of these lipid molecules in a phoP mutant partly accounts for its attenuated growth in macrophages and/or mice. To investigate the mechanism of regulation, here we demonstrate the essentiality of phosphorylation of PhoP in the regulation of complex lipid biosynthesis. We show that phosphorylated PhoP activates transcription of pks2 and msl3, gene(s) encoding polyketide β-ketoacyl synthases through direct DNA binding at the upstream regulatory region(s) of the target genes. Our results identify the genetic determinants recognized by PhoP and show that activation of target genes requires interaction(s) of the phosphorylated regulator at the cognate binding sites. The fact that these sites within the regulatory region of respective genes do not bind in vitro with either unphosphorylated or phosphorylation-deficient PhoP protein is consistent with phosphorylation-dependent assembly of the transcription initiation complex leading to in vivo transcriptional activation. Together, these results reveal so far unknown molecular mechanisms of how PhoP contributes to M. tuberculosis cell wall composition by regulating complex lipid biosynthesis.

Indexed as

Bacterial ProteinsCell WallFatty Acid SynthasesLipidsMycobacterium tuberculosisPhosphorylationResponse ElementsTranscription, GeneticBacterial ProteinsFatty Acid SynthasesLipidsPhoP protein, BacteriaPks2 protein, Mycobacterium tuberculosis

Identifiers

PMID22072719
PMCPMC3247998
OpenAlexW1967662130

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.