Evidence map›Paper›PMID 19233928›Full record

ArticleJournal of bacteriology2009

Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins.

Mark D Gonzalez, Jon Beckwith

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

42 citing papers in PubMed, 57 citations in OpenAlex.

  1. Defining the order of assembly of theJournal of bacteriology · 2026
    Article
  2. Article
  3. Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Transcriptomic and proteomic ramifications of segmental amplification inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. FtsA acts through FtsW to promote cell wall synthesis during cell division inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. PersistenteLife · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Mark D GonzalezDepartment of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
Jon Beckwith
Harvard University · US

Funding

MEMBRANE PROTEINS INVOLVED IN CELL DIVISION IN E.COLIR01GM038922 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BECKWITH, JONATHAN · 1987 to 2005
$2.1M
INSERTION AND TOPOLOGY OF MEMBRANE PROTEINSR37GM038922 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BECKWITH, JONATHAN R · 1987 to 1996
–
NIGMS NIH HHS GM38922NIGMS NIH HHS R01 GM038922
6 · The paper itself

Abstract

Cell division in bacteria requires the coordinated action of a set of proteins, the divisome, for proper constriction of the cell envelope. Multiple protein-protein interactions are required for assembly of a stable divisome. Within the Escherichia coli divisome is a conserved subcomplex of inner membrane proteins, the FtsB/FtsL/FtsQ complex, which is necessary for linking the upstream division proteins, which are predominantly cytoplasmic, with the downstream division proteins, which are predominantly periplasmic. FtsB and FtsL are small bitopic membrane proteins with predicted coiled-coil motifs, which themselves form a stable subcomplex that can recruit downstream division proteins independently of FtsQ; however, the details of how FtsB and FtsL interact together and with other proteins remain to be characterized. Despite the small size of FtsB, we identified separate interaction domains of FtsB that are required for interaction with FtsL and FtsQ. The N-terminal half of FtsB is necessary for interaction with FtsL and sufficient, when in complex with FtsL, for recruitment of downstream division proteins, while a portion of the FtsB C terminus is necessary for interaction with FtsQ. These properties of FtsB support the proposal that its main function is as part of a molecular scaffold to allow for proper formation of the divisome.

Indexed as

Cell DivisionProtein Interaction Domains and MotifsCell Cycle ProteinsEscherichia coliEscherichia coli ProteinsMembrane ProteinsProtein Interaction MappingSequence DeletionCell Cycle ProteinsEscherichia coli ProteinsFtsB protein, E coliftsL protein, E coliFtsQ protein, E coliMembrane Proteins

Identifiers

PMID19233928
PMCPMC2668415
OpenAlexW2135807487

What OpenQuestion holds

Textmetadata
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.