Evidence map›Paper›PMID 23974211›Full record

ArticleThe Journal of biological chemistry2013

SpoIIIE protein achieves directional DNA translocation through allosteric regulation of ATPase activity by an accessory domain.

Marina Besprozvannaya, Valerie L Pivorunas, Zachary Feldman, Briana M Burton

Open access · hybridAbstract 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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Milestones inMicrobial cell (Graz, Austria) · 2020
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Using a system's equilibrium behavior to reduce its energy dissipation in nonequilibrium processes.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  10. Molecular switch-like regulation in motor proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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

4 authors at 1 institution in 1 country.

Marina BesprozvannayaFrom the Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138.
Valerie L Pivorunas
Zachary Feldman
Briana M Burton
Harvard University · US

Funding

Training in Molecular, Cellular, and Chemical BiologyT32GM007598 · NIGMS · HARVARD UNIVERSITY · PI DULAC, CATHERINE · 1985 to 2019
$16.2M
NIGMS NIH HHS GM-07598NIGMS NIH HHS T32 GM007598
6 · The paper itself

Abstract

Bacterial chromosome segregation utilizes highly conserved directional translocases of the SpoIIIE/FtsK family. These proteins employ an accessory DNA-binding domain (γ) to dictate directionality of DNA transport. It remains unclear how the interaction of γ with specific recognition sequences coordinates directional DNA translocation. We demonstrate that the γ domain of SpoIIIE inhibits ATPase activity of the motor domain in the absence of DNA but stimulates ATPase activity through sequence-specific DNA recognition. Furthermore, we observe that communication between γ subunits is necessary for both regulatory roles. Consistent with these findings, the γ domain is necessary for robust DNA transport along the length of the chromosome in vivo. Together, our data reveal that directional activation involves allosteric regulation of ATP turnover through coordinated action of γ domains. Thus, we propose a coordinated stimulation model in which γ-γ communication is required to translate DNA sequence information from each γ to its respective motor domain.

Indexed as

Adenosine TriphosphatasesAllosteric RegulationAmino Acid MotifsAmino Acid SequenceBacillus subtilisBacterial ProteinsBiological TransportDNA, BacterialMolecular Sequence DataMutationProtein BindingProtein Structure, TertiaryProtein SubunitsStructure-Activity RelationshipAdenosine TriphosphatasesBacterial ProteinsDNA, BacterialProtein Subunitsspore-specific proteins, BacillusAllosteric RegulationATPasesChromosomesDNA-Protein InteractionMolecular Motors

Identifiers

PMID23974211
PMCPMC3789994
OpenAlexW2072029159

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.