Evidence map›Paper›PMID 26099469›Full record

ArticleNature communications2015

The bacterial tubulin FtsZ requires its intrinsically disordered linker to direct robust cell wall construction.

Kousik Sundararajan, Amanda Miguel, Samantha M Desmarais, Elizabeth L Meier, Kerwyn Casey Huang, Erin D Goley

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
12.5field-weighted citation impact, top 1% 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

54 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. GTPase activity regulates FtsZ ring positioning inMolecular biology of the cell · 2024
    Article
  8. Review
  9. Article
  10. 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
  11. Connecting sequence features within the disordered C-terminal linker ofProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. FtsZ dynamics in bacterial division: What, how, and why?Current opinion in cell biology · 2021
    Review
  16. Article
  17. Review
  18. Article
  19. Bacterial cell division at a glance.Journal of cell science · 2020
    Review
  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

6 authors at 2 institutions in 1 country.

Kousik SundararajanDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Amanda MiguelDepartment of Bioengineering, Stanford University, Stanford, California 94305, USA.
Samantha M DesmaraisDepartment of Bioengineering, Stanford University, Stanford, California 94305, USA.
Elizabeth L MeierDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Kerwyn Casey Huang1] Department of Bioengineering, Stanford University, Stanford, California 94305, USA [2] Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California 94305, USA.
Erin D GoleyDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.ORCID 0000000285182303
Johns Hopkins University · USStanford University · US

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
Molecular Biophysics Training Program at StanfordT32GM008294 · NIGMS · STANFORD UNIVERSITY · PI HUANG, KERWYN C. · 1989 to 2019
$7.4M
Engineering of cell shape and intracellular organizationDP2OD006466 · OD · STANFORD UNIVERSITY · PI HUANG, KERWYN C. · 2009 to 2009
$2.4M
NIGMS NIH HHS T32 GM007445NIGMS NIH HHS T32 GM008294NIH HHS DP2 OD006466
6 · The paper itself

Abstract

The bacterial GTPase FtsZ forms a cytokinetic ring at midcell, recruits the division machinery and orchestrates membrane and peptidoglycan cell wall invagination. However, the mechanism for FtsZ regulation of peptidoglycan metabolism is unknown. The FtsZ GTPase domain is separated from its membrane-anchoring C-terminal conserved (CTC) peptide by a disordered C-terminal linker (CTL). Here we investigate CTL function in Caulobacter crescentus. Strikingly, production of FtsZ lacking the CTL (ΔCTL) is lethal: cells become filamentous, form envelope bulges and lyse, resembling treatment with β-lactam antibiotics. This phenotype is produced by FtsZ polymers bearing the CTC and a CTL shorter than 14 residues. Peptidoglycan synthesis still occurs downstream of ΔCTL; however, cells expressing ΔCTL exhibit reduced peptidoglycan crosslinking and longer glycan strands than wild type. Importantly, midcell proteins are still recruited to sites of ΔCTL assembly. We propose that FtsZ regulates peptidoglycan metabolism through a CTL-dependent mechanism that extends beyond simple protein recruitment.

Indexed as

Caulobacter crescentusCell DivisionCell ShapeBacterial ProteinsCell WallCytoskeletal ProteinsImmunoblottingIntrinsically Disordered ProteinsMicroscopyMicroscopy, Electron, TransmissionPeptidoglycanPolymerizationBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaIntrinsically Disordered ProteinsPeptidoglycan

Identifiers

PMID26099469
PMCPMC4532373
OpenAlexW838493154

What OpenQuestion holds

Textmetadata
LicenceTDM
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.