Evidence map›Paper›PMID 25382687›Full record

ArticleMolecular microbiology2015

Oligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA.

Shishen Du, Kyung-Tae Park, Joe Lutkenhaus

Abstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. High-throughput discovery of inhibitory protein fragments with AlphaFold.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. High-throughput discovery of inhibitory protein fragments with AlphaFold.bioRxiv : the preprint server for biology · 2024
    Article
  5. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  14. Review
  15. FtsZ filaments have the opposite kinetic polarity of microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. 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

3 authors.

Shishen DuDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, KS, 66160, USA.
Kyung-Tae Park
Joe Lutkenhaus

Funding

REGULATION OF CELL DIVISIONR37GM029764 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI LUTKENHAUS, JOSEPH F · 2000 to 2010
$4.8M
REGULATION OF EXPRESSION OF CELL DIVISION GENESR01GM029764 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI LUTKENHAUS, JOSEPH F · 1985 to 2022
$4.2M
NIGMS NIH HHS GM 29764NIGMS NIH HHS R01 GM029764NIGMS NIH HHS R37 GM029764
6 · The paper itself

Abstract

A short conserved motif located at the carboxy terminus of FtsZ, referred to here as the CCTP (conserved carboxy-terminal peptide), is required for the interaction of FtsZ with many of its partners. In Escherichia coli interaction of FtsZ with its membrane anchors, ZipA and FtsA, as well as the spatial regulators of Z-ring formation, MinC and SlmA, requires the CCTP. ZipA interacts with FtsZ with high affinity and interacts with the CCTP with low affinity, but the reason for this difference is not clear. In this study, we show that this difference is due to the oligomerization of FtsZ converting the CCTP to a multivalent ligand that binds multiple ZipAs bound to a surface with high avidity. Artificial dimerization of the CCTP is sufficient to increase the affinity for ZipA in vitro. Similar principles apply to the interaction of FtsZ with SlmA. Although done in vitro, these results have implications for the recruitment of FtsZ to the membrane in vivo, the interaction of FtsZ with spatial regulators and the reconstitution of FtsZ systems in vitro.

Indexed as

Bacterial ProteinsCarrier ProteinsCell Cycle ProteinsCell DivisionCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsLigandsMembrane ProteinsProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationBacterial ProteinsCarrier ProteinsCell Cycle ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsZ protein, BacteriaLigandsMembrane ProteinsSlmA protein, E coliZipA protein, E coli

Identifiers

PMID25382687
PMCPMC4364296

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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.