Evidence map›Paper›PMID 31550057›Full record

ArticleMolecular microbiology2019

A PopZ-linked apical recruitment assay for studying protein-protein interactions in the bacterial cell envelope.

Hoong Chuin Lim, Thomas G Bernhardt

Abstract read
In one paragraph

Article in Molecular microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Structural modeling reveals the allosteric switch controlling the chitin utilization program ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Probing Pairwise Protein-Protein Interactions with the Bacterial POLAR Assay.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. FtsEX-independent control of RipA-mediated cell separation inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Review
  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

2 authors.

Hoong Chuin LimDepartment of Microbiology, Harvard Medical School, Boston, MA, 02115, USA.
Thomas G BernhardtDepartment of Microbiology, Harvard Medical School, Boston, MA, 02115, USA.ORCID 0000-0003-3566-7756

Funding

Peptidoglycan Biogenesis in Escherichia ColiR01AI083365 · NIAID · HARVARD MEDICAL SCHOOL · PI Thomas G Bernhardt · 2010 to 2026
$8.3M
NIAID NIH HHS R01 AI083365
6 · The paper itself

Abstract

Most bacteria are surrounded by a complex cell envelope. As with many biological processes, studies of envelope assembly have benefited from cell-based assays for detecting protein-protein interactions. These assays use simple readouts and lack a protein purification requirement, making them ideal for early stage investigations. The most widely used two-hybrid interaction assay for proteins involved in envelope biogenesis is based on the reconstitution of adenylate cyclase activity from a split enzyme. Because adenylate cyclase is only functional in the cytoplasm, both protein fusions used in the assay must have a terminus located in this compartment. However, many envelope assembly factors are wholly extracytoplasmic. Detecting interactions involving such proteins using two-hybrid systems has therefore been problematic. To address this issue, we developed a cytological assay in Escherichia coli based on PopZ from Caulobacter crescentus. Here, we demonstrate the utility of this PopZ-Linked Apical Recruitment (POLAR) method for detecting interactions between proteins located in different cellular compartments. Additionally, we report that recruitment of an active peptidoglycan synthase to the cell pole is detrimental for E. coli and that interactions between proteins in the inner and outer membranes of the Gram-negative envelope may provide a mechanism for recruiting protein complexes to subpolar sites.

Indexed as

Bacterial Outer MembraneBacterial Outer Membrane ProteinsBacterial ProteinsCaulobacter crescentusCell CycleCell Cycle ProteinsCell DivisionCell MembraneCell WallCentromereChromosomes, BacterialCytoplasmEscherichia coliPeptidoglycanProtein Interaction MappingProtein Interaction MapsBacterial Outer Membrane ProteinsBacterial ProteinsCell Cycle ProteinsPeptidoglycan

Identifiers

PMID31550057
PMCPMC7218919

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Registered trials

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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.