Evidence map›Paper›PMID 19748346›Full record

ArticleStructure (London, England : 1993)2009

Structural polymorphism of the ParM filament and dynamic instability.

Vitold E Galkin, Albina Orlova, Chris Rivera, R Dyche Mullins, Edward H Egelman

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Archaeal actin from a hyperthermophile forms a single-stranded filament.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  7. Article
  8. Review
  9. Structure of the ParM filament at 8.5Å resolution.Journal of structural biology · 2013
    Article
  10. Article
  11. The bacterial cytoskeleton: more than twisted filaments.Current opinion in cell biology · 2013
    Review
  12. Article
  13. Are ParM filaments polar or bipolar?Journal of molecular biology · 2012
    Article
  14. Article
  15. Article
  16. Novel actin-like filament structure from Clostridium tetani.The Journal of biological chemistry · 2012
    Article
  17. Article
  18. Actin filaments as tension sensors.Current biology : CB · 2012
    Review
  19. Article
  20. Actin structure and function.Annual review of biophysics · 2011
    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

5 authors.

Vitold E GalkinDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908-0733, USA. galkin@virginia.edu
Albina Orlova
Chris Rivera
R Dyche Mullins
Edward H Egelman

Funding

MECHANISMS OF ARP2/3 ACTIVATION AND FUNCTIONR01GM061010 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MULLINS, R DYCHE · 2000 to 2015
$3.8M
Structural Studies of ActinR01GM081303 · NIGMS · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2007 to 2016
$3.6M
NIGMS NIH HHS GM081303NIGMS NIH HHS GM61010NIGMS NIH HHS R01 GM061010NIGMS NIH HHS R01 GM081303
6 · The paper itself

Abstract

Segregation of the R1 plasmid in bacteria relies on ParM, an actin homolog that segregates plasmids by switching between cycles of polymerization and depolymerization. We find similar polymerization kinetics and stability in the presence of either ATP or GTP and a 10-fold affinity preference for ATP over GTP. We used electron cryo-microscopy to evaluate the heterogeneity within ParM filaments. In addition to variable twist, ParM has variable axial rise, and both parameters are coupled. Subunits in the same ParM filaments can exist in two different structural states, with the nucleotide-binding cleft closed or open, and the bound nucleotide biases the distribution of states. The interface between protomers is different between these states, and in neither state is it similar to F-actin. Our results suggest that the closed state of the cleft is required but not sufficient for ParM polymerization, and provide a structural basis for the dynamic instability of ParM filaments.

Indexed as

ActinsAdenosine TriphosphateCryoelectron MicroscopyEscherichia coli ProteinsGuanosine TriphosphateHydrolysisModels, MolecularProtein ConformationActinsAdenosine TriphosphateEscherichia coli ProteinsGuanosine TriphosphateParM protein, E coli

Identifiers

PMID19748346
PMCPMC2745721

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.