Evidence map›Paper›PMID 29889022›Full record

ArticleeLife2018

Lateral interactions between protofilaments of the bacterial tubulin homolog FtsZ are essential for cell division.

Fenghui Guan, Jiayu Yu, Jie Yu, Yang Liu, Ying Li, Xin-Hua Feng, Kerwyn Casey Huang, Zengyi Chang, Sheng Ye

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

21 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
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  7. MipZ caps the plus-end of FtsZ polymers to promote their rapid disassembly.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Connecting sequence features within the disordered C-terminal linker ofProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Bacterial cell division at a glance.Journal of cell science · 2020
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
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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 3 institutions in 2 countries.

Fenghui Guan *Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China.ORCID http://orcid.org/0000-0002-2756-5736
Jiayu Yu *The State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China.
Jie Yu *Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China.
Yang Liu *The State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China.
Ying Li *Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China.
Xin-Hua FengInnovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China.
Kerwyn Casey HuangDepartment of Bioengineering, Stanford University, Stanford, United States.
Zengyi ChangThe State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China.
Sheng YeInnovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China.ORCID http://orcid.org/0000-0001-9300-6257
Peking University · CNZhejiang Lab · CNChan Zuckerberg Initiative (United States) · US

Funding

TRAINING & OUTREACH COREP50GM107615 · NIGMS · STANFORD UNIVERSITY · PI FERRELL, JAMES E. · 2013 to 2017
$10.9M
NIGMS NIH HHS P50 GM107615
6 · The paper itself

Abstract

The prokaryotic tubulin homolog FtsZ polymerizes into protofilaments, which further assemble into higher-order structures at future division sites to form the Z-ring, a dynamic structure essential for bacterial cell division. The precise nature of interactions between FtsZ protofilaments that organize the Z-ring and their physiological significance remain enigmatic. In this study, we solved two crystallographic structures of a pair of FtsZ protofilaments, and demonstrated that they assemble in an antiparallel manner through the formation of two different inter-protofilament lateral interfaces. Our in vivo photocrosslinking studies confirmed that such lateral interactions occur in living cells, and disruption of the lateral interactions rendered cells unable to divide. The inherently weak lateral interactions enable FtsZ protofilaments to self-organize into a dynamic Z-ring. These results have fundamental implications for our understanding of bacterial cell division and for developing antibiotics that target this key process.

Indexed as

Amino Acid SequenceBacterial ProteinsCell DivisionComputer SimulationCrystallography, X-RayCytoskeletal ProteinsEscherichia coliMicrofilament ProteinsModels, MolecularProtein BindingProtein ConformationSequence Homology, Amino AcidTubulinBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaMicrofilament ProteinsTubulincell biologycrystal structureE. coliFtsZ protofilamentlateral interfacemolecular biophysicsphotocrosslinkingstructural biologyZ ring

Identifiers

PMID29889022
PMCPMC6050046
OpenAlexW2808171107

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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.