Evidence map›Paper›PMID 22431591›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP.

Katrin Beilharz, Linda Nováková, Daniela Fadda, Pavel Branny, Orietta Massidda, Jan-Willem Veening

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
10.7field-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

97 citing papers in PubMed, 176 citations in OpenAlex.

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  8. Bacterial extracellular vesicles target different bacterial species, impairing cell division and diminishing their pathogenicity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  11. How do spherical bacteria regulate cell division?Biochemical Society transactions · 2025
    Review
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37 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

6 authors at 3 institutions in 3 countries.

Katrin BeilharzMolecular Genetics Group, Groningen Biomolecular Sciences and Biotechnology Institute, Centre for Synthetic Biology, University of Groningen, 9747 AG, Groningen, The Netherlands.
Linda Nováková
Daniela Fadda
Pavel Branny
Orietta Massidda
Jan-Willem Veening
Czech Academy of Sciences · CZUniversity of Cagliari · ITUniversity of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

How the human pathogen Streptococcus pneumoniae coordinates cell-wall synthesis during growth and division to achieve its characteristic oval shape is poorly understood. The conserved eukaryotic-type Ser/Thr kinase of S. pneumoniae, StkP, previously was reported to phosphorylate the cell-division protein DivIVA. Consistent with a role in cell division, GFP-StkP and its cognate phosphatase, GFP-PhpP, both localize to the division site. StkP localization depends on its penicillin-binding protein and Ser/Thr-associated domains that likely sense uncross-linked peptidoglycan, because StkP and PhpP delocalize in the presence of antibiotics that target the latest stages of cell-wall biosynthesis and in cells that have stopped dividing. Time-lapse microscopy shows that StkP displays an intermediate timing of recruitment to midcell: StkP arrives shortly after FtsA but before DivIVA. Furthermore, StkP remains at midcell longer than FtsA, until division is complete. Cells mutated for stkP are perturbed in cell-wall synthesis and display elongated morphologies with multiple, often unconstricted, FtsA and DivIVA rings. The data show that StkP plays an important role in regulating cell-wall synthesis and controls correct septum progression and closure. Overall, our results indicate that StkP signals information about the cell-wall status to key cell-division proteins and in this way acts as a regulator of cell division.

Indexed as

Cell DivisionConserved SequenceAnti-Bacterial AgentsBacterial ProteinsCell ProliferationCell WallEnzyme ActivationExtracellular SpaceGreen Fluorescent ProteinsHumansLigandsModels, BiologicalPhosphorylationProtein Serine-Threonine KinasesProtein Structure, TertiaryProtein TransportAnti-Bacterial AgentsBacterial ProteinsGreen Fluorescent ProteinsLigandsProtein Serine-Threonine KinasesRecombinant Fusion Proteins

Identifiers

PMID22431591
PMCPMC3326482
OpenAlexW2116857869

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.