Evidence map›Paper›PMID 23824192›Full record

ArticleThe Journal of biological chemistry2013

Rapid in vitro assembly of Caulobacter crescentus FtsZ protein at pH 6.5 and 7.2.

Sara L Milam, Harold P Erickson

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Evidence of conformational switch in Streptococcus pneumoniae FtsZ during polymerization.Protein science : a publication of the Protein Society · 2021
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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.

Sara L MilamDepartment of Cell Biology, Duke University Medical Center, Durham, North Carolina 27701-3709, USA.
Harold P Erickson

Funding

Structure and Assembly Dynamics of FtsZR01GM066014 · NIGMS · DUKE UNIVERSITY · PI ERICKSON, HAROLD P · 2002 to 2018
$7.5M
NIGMS NIH HHS GM66014NIGMS NIH HHS R01 GM066014
6 · The paper itself

Abstract

FtsZ from most bacteria assembles rapidly in vitro, reaching a steady-state plateau in 5-10 s after addition of GTP. A recent study used a novel dynamic light-scattering technique to assay the assembly of FtsZ from Caulobacter crescentus (CcFtsZ) and reported that assembly required 10 min, ∼100 times slower than for related bacteria. Previous studies had indicated normal, rapid assembly of CcFtsZ. We have reinvestigated the assembly kinetics using a mutant L72W, where assembly of subunits into protofilaments results in a significant increase in tryptophan fluorescence. We found that assembly reached a plateau in 5-10 s and showed no change in the following 10 min. This was confirmed by 90° light scattering and negative-stain electron microscopy. The very slow kinetics in the dynamic light-scattering study may be related to a refractory state induced when the FtsZ protein is stored without nucleotide, a phenomenon that we had observed in a previous study of EcFtsZ. We conclude that CcFtsZ is not an outlier, but shows rapid assembly kinetics similar to FtsZ from related bacteria.

Indexed as

Bacterial ProteinsCaulobacter crescentusCytoskeletal ProteinsFluorescenceGTP PhosphohydrolasesGuanosine TriphosphateHydrogen-Ion ConcentrationHydrolysisKineticsMagnesiumNegative StainingScattering, RadiationBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaGTP PhosphohydrolasesGuanosine TriphosphateMagnesiumBacteriaCell DivisionElectron Microscopy (EM)FluorescenceGTPaseTubulin

Identifiers

PMID23824192
PMCPMC3745314

What OpenQuestion holds

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Registered trials

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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.