Evidence map›Paper›PMID 27525505›Full record

ArticleNature2016

SEDS proteins are a widespread family of bacterial cell wall polymerases.

Alexander J Meeske, Eammon P Riley, William P Robins, Tsuyoshi Uehara, John J Mekalanos, Daniel Kahne, Suzanne Walker, Andrew C Kruse, Thomas G Bernhardt, David Z Rudner

Open access · greenAbstract read
In one paragraph

Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 319 papers.

0numbers the graph read from it
0cells of the map it votes in
319citing papers in PubMed
55.8field-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

319 citing papers in PubMed, 521 citations in OpenAlex.

  1. Defining the order of assembly of theJournal of bacteriology · 2026
    Article
  2. Article
  3. mBio · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. A broadly conserved gram-positive lipoprotein regulates cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. bioRxiv : the preprint server for biology · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

259 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Alexander J MeeskeDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.
Eammon P RileyDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.
William P RobinsDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.
Tsuyoshi UeharaDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.
John J MekalanosDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.
Daniel KahneDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 250 Longwood Ave, Boston, Massachusetts 02115, USA.
Suzanne WalkerDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.
Andrew C KruseDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 250 Longwood Ave, Boston, Massachusetts 02115, USA.
Thomas G BernhardtDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.
David Z RudnerDepartment of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.
Harvard University · US

Funding

Targeting bacterial cell wall biogenesis for the development of novel antimicrobU19AI109764 · NIAID · HARVARD MEDICAL SCHOOL · PI KASPER, DENNIS L. · 2014 to 2018
$25.2M
Genetic analysis of toxinogenesis of Vibrio choleraeR37AI018045 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI John Joseph Mekalanos · 1989 to 2026
$12.8M
INFECTIOUS DISEASE AND BASIC MICROBIOLOGICAL MECHANISMST32AI007061 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI Marcia B Goldberg · 1985 to 2026
$12.1M
Peptidoglycan Biogenesis in Escherichia ColiR01AI083365 · NIAID · HARVARD MEDICAL SCHOOL · PI Thomas G Bernhardt · 2010 to 2026
$8.3M
Genetic Analysis of Toxinogenesis in Vibrio CholeraeR01AI018045 · NIAID · HARVARD MEDICAL SCHOOL · PI MEKALANOS, JOHN JOSEPH · 2009 to 2018
$6.7M
Mechanism and Inhibition of Enzymes that Assemble Bacterial Cell WallR01GM076710 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALKER, SUZANNE · 2007 to 2019
$5.9M
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
Membrane Remodeling and Protein Trafficking in BacteriaR01GM073831 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI RUDNER, DAVID Z · 2005 to 2014
$3.4M
A multidisciplinary approach to elucidating gene function in a model Gram-positivRC2GM092616 · NIGMS · HARVARD MEDICAL SCHOOL · PI RUDNER, DAVID Z · 2009 to 2010
$2.0M
NIAID NIH HHS R01 AI083365NIAID NIH HHS R01 AI099144NIAID NIH HHS R37 AI018045NIAID NIH HHS T32 AI007061NIAID NIH HHS U19 AI109764NIGMS NIH HHS R01 GM073831NIGMS NIH HHS R01 GM076710NIGMS NIH HHS RC2 GM092616
6 · The paper itself

Abstract

Elongation of rod-shaped bacteria is mediated by a dynamic peptidoglycan-synthetizing machinery called the Rod complex. Here we report that, in Bacillus subtilis, this complex is functional in the absence of all known peptidoglycan polymerases. Cells lacking these enzymes survive by inducing an envelope stress response that increases the expression of RodA, a widely conserved core component of the Rod complex. RodA is a member of the SEDS (shape, elongation, division and sporulation) family of proteins, which have essential but ill-defined roles in cell wall biogenesis during growth, division and sporulation. Our genetic and biochemical analyses indicate that SEDS proteins constitute a family of peptidoglycan polymerases. Thus, B. subtilis and probably most bacteria use two distinct classes of polymerase to synthesize their exoskeleton. Our findings indicate that SEDS family proteins are core cell wall synthases of the cell elongation and division machinery, and represent attractive targets for antibiotic development.

Indexed as

PolymerizationAnti-Bacterial AgentsBacillus subtilisBacterial ProteinsCell DivisionCell WallDrug DesignDrug Resistance, BacterialMutationOligosaccharidesPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan GlycosyltransferasePhenotypeAnti-Bacterial AgentsBacterial ProteinsmoenomycinOligosaccharidesPenicillin-Binding ProteinsPeptidoglycanPeptidoglycan Glycosyltransferase

Identifiers

PMID27525505
PMCPMC5161649
OpenAlexW2517176893

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.