Evidence map›Paper›PMID 21190553›Full record

ArticleBMC microbiology2010

Regulation of polar peptidoglycan biosynthesis by Wag31 phosphorylation in mycobacteria.

Charul Jani, Hyungjin Eoh, Jae Jin Lee, Khozima Hamasha, Moodakare Bheema Sahana, Jeong-Sun Han, Seeta Nyayapathy, Jung-Yeon Lee, Joo-Won Suh, Sang Hee Lee and 3 more

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

63 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
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  11. Molecular Mechanisms of MmpL3 Function and Inhibition.Microbial drug resistance (Larchmont, N.Y.) · 2023
    Review
  12. Review
  13. Types and functions of heterogeneity in mycobacteria.Nature reviews. Microbiology · 2022
    Review
  14. Article
  15. Article
  16. Localization of EccABMC microbiology · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. Article

3 more citing papers are in PubMed but not listed here.

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

13 authors at 3 institutions in 2 countries.

Charul JaniDepartment of Biological Science, Wayne State University, 5047 Gullen Mall, Detroit, MI 48202, USA.
Hyungjin Eoh
Jae Jin Lee
Khozima Hamasha
Moodakare Bheema Sahana
Jeong-Sun Han
Seeta Nyayapathy
Jung-Yeon Lee
Joo-Won Suh
Sang Hee Lee
Steve J Rehse
Dean C Crick
Choong-Min Kang
Wayne State University · USMyongji University · KRColorado State University · US

Funding

Sterol/Hopanoid Biosynthesis: An Anti-TB Drug TargetR01AI049151 · NIAID · COLORADO STATE UNIVERSITY-FORT COLLINS · PI CRICK, DEAN C · 2001 to 2019
$4.1M
NIAID NIH HHS R01AI049151
6 · The paper itself

Abstract

backgroundSensing and responding to environmental changes is a central aspect of cell division regulation. Mycobacterium tuberculosis contains eleven Ser/Thr kinases, two of which, PknA and PknB, are key signaling molecules that regulate cell division/morphology. One substrate of these kinases is Wag31, and we previously showed that partial depletion of Wag31 caused morphological changes indicative of cell wall defects, and that the phosphorylation state of Wag31 affected cell growth in mycobacteria. In the present study, we further characterized the role of the Wag31 phosphorylation in polar peptidoglycan biosynthesis.

resultsWe demonstrate that the differential growth among cells expressing different wag31 alleles (wild-type, phosphoablative, or phosphomimetic) is caused by, at least in part, dissimilar nascent peptidoglycan biosynthesis. The phosphorylation state of Wag31 is found to be important for protein-protein interactions between the Wag31 molecules, and thus, for its polar localization. Consistent with these results, cells expressing a phosphomimetic wag31 allele have a higher enzymatic activity in the peptidoglycan biosynthetic pathway.

conclusionsThe Wag31Mtb phosphorylation is a novel molecular mechanism by which Wag31Mtb regulates peptidoglycan synthesis and thus, optimal growth in mycobacteria.

Indexed as

Bacterial ProteinsGene Expression Regulation, BacterialMycobacterium smegmatisPeptidoglycanPhosphorylationProtein TransportBacterial ProteinsPeptidoglycan

Identifiers

PMID21190553
PMCPMC3019181
OpenAlexW2127915701

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.