Evidence map›Paper›PMID 19527070›Full record

ArticleBiochemistry2009

FtsZ filament dynamics at steady state: subunit exchange with and without nucleotide hydrolysis.

Yaodong Chen, Harold P Erickson

Abstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.0field-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

49 citing papers in PubMed, 74 citations in OpenAlex.

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  16. FtsZ filaments have the opposite kinetic polarity of microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Article
  18. Efficient models of polymerization applied to FtsZ ring assembly inProceedings of the National Academy of Sciences of the United States of America · 2018
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  19. Review
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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.

Yaodong ChenDepartment of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710-3709, USA.
Harold P Erickson
Duke Medical Center · US

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

We have measured three aspects of FtsZ filament dynamics at steady state: rates of GTP hydrolysis, subunit exchange between protofilaments, and disassembly induced by dilution or excess GDP. All three reactions were slowed with an increase in the potassium concentration from 100 to 500 mM, via replacement of potassium with rubidium, or with an increase in the magnesium concentration from 5 to 20 mM. Electron microscopy showed that the polymers assembled under the conditions of fastest assembly were predominantly short, one-stranded protofilaments, whereas under conditions of slower dynamics, the protofilaments tended to associate into long, thin bundles. We suggest that exchange of subunits between protofilaments at steady state involves two separate mechanisms: (1) fragmentation or dissociation of subunits from protofilament ends following GTP hydrolysis and (2) reversible association and dissociation of subunits from protofilament ends independent of hydrolysis. Exchange of nucleotides on these recycling subunits could give the appearance of exchange directly into the polymer. Several of our observations suggest that exchange of nucleotide can take place on these recycling subunits, but not directly into the FtsZ polymer. Annealing of protofilaments was demonstrated for the L68W mutant in EDTA buffer but not in Mg buffer, where rapid cycling of subunits may obscure the effect of annealing. We also reinvestigated the nucleotide composition of FtsZ polymers at steady state. We found that the GDP:GTP ratio was 50:50 for concentrations of GTP >100 microM, significantly higher than the 20:80 ratio previously reported at 20 microM GTP.

Indexed as

Actin CytoskeletonAmino Acid SubstitutionBacterial ProteinsBuffersCytoskeletal ProteinsEscherichia coliFluorescence Resonance Energy TransferGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateHydrolysisKineticsMagnesiumPotassiumProtein SubunitsRubidiumBacterial ProteinsBuffersCytoskeletal ProteinsFtsZ protein, BacteriaGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateMagnesiumPotassiumProtein SubunitsRubidium

Identifiers

PMID19527070
PMCPMC2796084
OpenAlexW1965508308

What OpenQuestion holds

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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.