Evidence map›Paper›PMID 22610443›Full record

ArticleThe Journal of biological chemistry2012

Septal localization of the Mycobacterium tuberculosis MtrB sensor kinase promotes MtrA regulon expression.

Renata Plocinska, Gorla Purushotham, Krishna Sarva, Indumathi S Vadrevu, Emmanuel V P Pandeeti, Naresh Arora, Przemyslaw Plocinski, Murty V Madiraju, Malini Rajagopalan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

42 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
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  3. An activator of a two-component system controls cell separation and intrinsic drug resistance inProceedings of the National Academy of Sciences of the United States of America · 2026
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  8. Regulatory role ofFrontiers in microbiology · 2024
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  11. Article
  12. Article
  13. Review
  14. Article
  15. Point mutation in the stop codon ofMicrobiology (Reading, England) · 2021
    Article
  16. Article
  17. Bacterial Protein Kinases.Advances in experimental medicine and biology · 2021
    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

9 authors at 1 institution in 1 country.

Renata PlocinskaBiomedical Research, The University of Texas Health Science Center, Tyler, Texas 75708-3154, USA.
Gorla Purushotham
Krishna Sarva
Indumathi S Vadrevu
Emmanuel V P Pandeeti
Naresh Arora
Przemyslaw Plocinski
Murty V Madiraju
Malini Rajagopalan
The University of Texas Health Science Center at Tyler · US

Funding

Mycobacterium tuberculosis cell division and proliferationR01AI048417 · NIAID · UNIVERSITY OF TEXAS HLTH CTR AT TYLER · PI RAJAGOPALAN, MALINI · 2000 to 2011
$3.0M
MYCOBACTERIUM TUBERCULOSIS REPLICATION AND PROLIFERATIONR01AI084734 · NIAID · UNIVERSITY OF TEXAS HLTH CTR AT TYLER · PI MADIRAJU, MURTY V. · 2009 to 2012
$1.4M
NIAID NIH HHS AI084734NIAID NIH HHS AI48417NIAID NIH HHS R01 AI048417NIAID NIH HHS R01 AI084734
6 · The paper itself

Abstract

The mechanisms responsible for activation of the MtrAB two-component regulatory signal transduction system, which includes sensor kinase MtrB and response regulator MtrA, are unknown. Here, we show that an MtrB-GFP fusion protein localized to the cell membrane, the septa, and the poles in Mycobacterium tuberculosis and Mycobacterium smegmatis. This localization was independent of MtrB phosphorylation status but dependent upon the assembly of FtsZ, the initiator of cell division. The M. smegmatis mtrB mutant was filamentous, defective for cell division, and contained lysozyme-sensitive cell walls. The mtrB phenotype was complemented by either production of MtrB protein competent for phosphorylation or overproduction of MtrA(Y102C) and MtrA(D13A) mutant proteins exhibiting altered phosphorylation potential, indicating that either MtrB phosphorylation or MtrB independent expression of MtrA regulon genes, including those involved in cell wall processing, are necessary for regulated cell division. In partial support of this observation, we found that the essential cell wall hydrolase ripA is an MtrA target and that the expression of bona fide MtrA targets ripA, fbpB, and dnaA were compromised in the mtrB mutant and partially rescued upon MtrA(Y102C) and MtrA(D13A) overproduction. MtrB septal assembly was compromised upon FtsZ depletion and exposure of cells to mitomycin C, a DNA damaging agent, which interferes with FtsZ ring assembly. Expression of MtrA targets was also compromised under the above conditions, indicating that MtrB septal localization and MtrA regulon expression are linked. We propose that MtrB septal association is a necessary feature of MtrB activation that promotes MtrA phosphorylation and MtrA regulon expression.

Indexed as

Gene Expression Regulation, BacterialATP-Binding Cassette TransportersBacterial ProteinsBlotting, WesternCell DivisionCell MembraneCell WallCytoskeletal ProteinsGreen Fluorescent ProteinsMicroscopy, FluorescenceMutationMycobacterium smegmatisMycobacterium tuberculosisPhosphorylationPhosphotransferasesRegulonATP-Binding Cassette TransportersBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaGreen Fluorescent ProteinsMtrA protein, BacteriaMtrB protein, BacteriaPhosphotransferasesRNA-Binding ProteinsTranscription Factors

Identifiers

PMID22610443
PMCPMC3390665
OpenAlexW2000240522

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.