Evidence map›Paper›PMID 30335755›Full record

ArticlePLoS genetics2018

A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery.

Patricia D A Rohs, Jackson Buss, Sue I Sim, Georgia R Squyres, Veerasak Srisuknimit, Mandy Smith, Hongbaek Cho, Megan Sjodt, Andrew C Kruse, Ethan C Garner and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
12.7field-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

102 citing papers in PubMed, 146 citations in OpenAlex.

  1. Article
  2. Article
  3. A broadly conserved gram-positive lipoprotein regulates cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Penicillin-Binding Proteins inAntibiotics (Basel, Switzerland) · 2026
    Review
  10. Article
  11. Conformational regulation of two essential activators of bacterial cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Twin-arginine transport complex plays an essential role inbioRxiv : the preprint server for biology · 2025
    Article
  13. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  14. Article
  15. Milestones in the development ofJournal of bacteriology · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

42 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.

Patricia D A RohsDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, United States of America.ORCID 0000-0003-4698-1820
Jackson BussDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, United States of America.
Sue I SimDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, United States of America.ORCID 0000-0003-3560-101X
Georgia R SquyresDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts, United States of America.ORCID 0000-0002-8717-2897
Veerasak SrisuknimitDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts, United States of America.
Mandy SmithDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, United States of America.ORCID 0000-0002-6958-9904
Hongbaek ChoDepartment of Biological Sciences, Sungkyunkwan University, Suwon, Gyeonggi, Korea.
Megan SjodtDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, United States of America.
Andrew C KruseDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, United States of America.ORCID 0000-0002-1467-1222
Ethan C GarnerDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts, United States of America.ORCID 0000-0003-0141-3555
Suzanne WalkerDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, United States of America.
Daniel E KahneDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts, United States of America.
Thomas G BernhardtDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, United States of America.ORCID 0000-0003-3566-7756
Harvard University · USHoward Hughes Medical Institute · USSungkyunkwan University · KR

Funding

Targeting bacterial cell wall biogenesis for the development of novel antimicrobU19AI109764 · NIAID · HARVARD MEDICAL SCHOOL · PI BELTZ, GERALD A · 2014 to 2018
$25.2M
Identifying and validating new antibiotic targets in cell wall synthesis pathwaysR01AI099144 · NIAID · HARVARD MEDICAL SCHOOL · PI BERNHARDT, THOMAS G, WALKER, SUZANNE · 2012 to 2016
$4.3M
Fluorescence Microscope for Time-Lapse Imaging of BacteriaS10RR027344 · NCRR · HARVARD MEDICAL SCHOOL · PI RUDNER, DAVID Z · 2010 to 2010
$162k
CIHRNCRR NIH HHS S10 RR027344NIAID NIH HHS R01 AI099144NIAID NIH HHS U19 AI109764
6 · The paper itself

Abstract

Cell elongation in rod-shaped bacteria is mediated by the Rod system, a conserved morphogenic complex that spatially controls cell wall assembly by the glycan polymerase RodA and crosslinking enzyme PBP2. Using Escherichia coli as a model system, we identified a PBP2 variant that promotes Rod system function when essential accessory components of the machinery are inactivated. This PBP2 variant hyperactivates cell wall synthesis in vivo and stimulates the activity of RodA-PBP2 complexes in vitro. Cells with the activated synthase also exhibited enhanced polymerization of the actin-like MreB component of the Rod system. Our results define an activation pathway governing Rod system function in which PBP2 conformation plays a central role in stimulating both glycan polymerization by its partner RodA and the formation of cytoskeletal filaments of MreB to orient cell wall assembly. In light of these results, previously isolated mutations that activate cytokinesis suggest that an analogous pathway may also control cell wall synthesis by the division machinery.

Indexed as

ActinsBacterial ProteinsCell CycleCell WallCytokinesisCytoskeletonEscherichia coliEscherichia coli ProteinsMembrane ProteinsMorphogenesisPenicillin-Binding ProteinsPeptidoglycanPolymerizationPolysaccharidesActinsBacterial ProteinsEscherichia coli ProteinsMembrane ProteinsMrdA protein, E colimrdB protein, E coliMreC protein, BacteriaPenicillin-Binding ProteinsPeptidoglycanPolysaccharides

Identifiers

PMID30335755
PMCPMC6207328
OpenAlexW2895954140

What OpenQuestion holds

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LicenceCC BY
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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.