Evidence map›Paper›PMID 18786147›Full record

ArticleMolecular microbiology2008

Localization of PBP3 in Caulobacter crescentus is highly dynamic and largely relies on its functional transpeptidase domain.

Teresa Costa, Richa Priyadarshini, Christine Jacobs-Wagner

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
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  10. Review
  11. Host plant peptides elicit a transcriptional response to control the Sinorhizobium meliloti cell cycle during symbiosis.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Article
  13. Article
  14. Divin: a small molecule inhibitor of bacterial divisome assembly.Journal of the American Chemical Society · 2013
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Advances in understanding E. coli cell fission.Current opinion in microbiology · 2010
    Review
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

3 authors at 2 institutions in 1 country.

Teresa CostaDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.
Richa Priyadarshini
Christine Jacobs-Wagner
Yale University · USHoward Hughes Medical Institute · US

Funding

Temporal and Spatial Control of the Cell Cycle in Caulobacter CrescentusR01GM065835 · NIGMS · YALE UNIVERSITY · PI JACOBS-WAGNER, CHRISTINE · 2003 to 2016
$3.7M
Intermediate filament cytoskeleton and cell shape in Caulobacter crescentusR01GM076698 · NIGMS · YALE UNIVERSITY · PI JACOBS-WAGNER, CHRISTINE · 2006 to 2009
$1.1M
Howard Hughes Medical InstituteNIGMS NIH HHS GM065835NIGMS NIH HHS GM076698NIGMS NIH HHS R01 GM065835NIGMS NIH HHS R01 GM076698
6 · The paper itself

Abstract

In rod-shaped bacteria, septal peptidoglycan synthesis involves the late recruitment of the ftsI gene product (PBP3 in Escherichia coli) to the FtsZ ring. We show that in Caulobacter crescentus, PBP3 accumulates at the new pole at the beginning of the cell cycle. Fluorescence recovery after photobleaching experiments reveal that polar PBP3 molecules are, constantly and independently of FtsZ, replaced by those present in the cellular pool, implying that polar PBP3 is not a remnant of the previous division. By the time cell constriction is initiated, all PBP3 polar accumulation has disappeared in favour of an FtsZ-dependent localization near midcell, consistent with PBP3 function in cell division. Kymograph analysis of time-lapse experiments shows that the recruitment of PBP3 to the FtsZ ring is progressive and initiated very early on, shortly after FtsZ ring formation and well before cell constriction starts. Accumulation of PBP3 near midcell is also highly dynamic with a rapid exchange of PBP3 molecules between midcell and cellular pools. Localization of PBP3 at both midcell and pole appears multifactorial, primarily requiring the catalytic site of PBP3. Collectively, our results suggest a role for PBP3 in pole morphogenesis and provide new insights into the process of peptidoglycan assembly during division.

Indexed as

Cell DivisionBacterial ProteinsCatalytic DomainCaulobacter crescentusCytoskeletal ProteinsKymographyPenicillin-Binding ProteinsPeptidyl TransferasesTime FactorsBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaPenicillin-Binding ProteinsPeptidyl Transferases

Identifiers

PMID18786147
PMCPMC2581642
OpenAlexW2096079692

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.