Evidence map›Paper›PMID 22385855›Full record

ArticleBiophysical journal2012

Using DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope.

M E Fuentes-Perez, E J Gwynn, M S Dillingham, F Moreno-Herrero

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2012. 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
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

19 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. The role of ATP-dependent machines in regulating genome topology.Current opinion in structural biology · 2016
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. An asymmetric SMC-kleisin bridge in prokaryotic condensin.Nature structural & molecular biology · 2013
    Article
  17. Breaking symmetry in SMCs.Nature structural & molecular biology · 2013
    Article
  18. Article
  19. 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

4 authors at 3 institutions in 2 countries.

M E Fuentes-PerezDepartment of Macromolecular Structures, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
E J Gwynn
M S Dillingham
F Moreno-Herrero
University of Bristol · GBCentro Nacional de Biotecnología · ESConsejo Superior de Investigaciones Científicas · ES

Funding

Wellcome Trust 077368
6 · The paper itself

Abstract

Atomic force microscopy can potentially provide information on protein volumes, shapes, and interactions but is susceptible to variable tip-induced artifacts. In this study, we present an atomic force microscopy approach that can measure volumes of nonglobular polypeptides such as structural maintenance of chromosomes (SMC) proteins, and use it to study the interactions that occur within and between SMC complexes. Together with the protein of interest, we coadsorb a DNA molecule and use it as a fiducial marker to account for tip-induced artifacts that affect both protein and DNA, allowing normalization of protein volumes from images taken on different days and with different tips. This approach significantly reduced the error associated with volume analysis, and allowed determination of the oligomeric states and architecture of the Bacillus subtilis SMC complex, formed by the SMC protein, and by the smaller ScpA and ScpB subunits. This work reveals that SMC and ScpB are dimers and that ScpA is a stable monomer. Moreover, whereas ScpA binds directly to SMC, ScpB only binds to SMC in the presence of ScpA. Notably, the presence of both ScpA and ScpB favored the formation of higher-order structures of SMC complexes, suggesting a role for these subunits in the organization of SMC oligomers.

Indexed as

Microscopy, Atomic ForceAdsorptionBacterial ProteinsCell Cycle ProteinsDNAMolecular ProbesMolecular WeightProtein MultimerizationProtein Structure, QuaternaryBacterial ProteinsCell Cycle ProteinsDNAMolecular ProbesScpA protein, Bacillus subtilisSMC protein, Bacteria

Identifiers

PMID22385855
PMCPMC3283809
OpenAlexW2002484801

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.