Evidence map›Paper›PMID 19262687›Full record

ArticlePloS one2009

The coiled coils of cohesin are conserved in animals, but not in yeast.

Glenn E White, Harold P Erickson

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.1field-weighted citation impact, top 47% 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

7 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Cohesin biology meets the loop extrusion model.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2017
    Review
  4. Article
  5. Review
  6. Article
  7. 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

2 authors at 2 institutions in 1 country.

Glenn E WhiteDepartment of Biological and Environmental Sciences, Longwood University, Farmville, Virginia, United Kingdom.
Harold P Erickson
Duke Medical Center · USLongwood University · US

Funding

EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINSR01CA047056 · NCI · DUKE UNIVERSITY · PI ERICKSON, HAROLD P · 1988 to 2016
$4.7M
EXTRACELLULAR MATRIX AND CELL ATTACHMENT PROTEINSR37CA047056 · NCI · DUKE UNIVERSITY · PI ERICKSON, HAROLD P · 1993 to 2000
$308k
NCI NIH HHS CA47056NCI NIH HHS R01 CA047056NCI NIH HHS R37 CA047056
6 · The paper itself

Abstract

backgroundThe SMC proteins are involved in DNA repair, chromosome condensation, and sister chromatid cohesion throughout Eukaryota. Long, anti-parallel coiled coils are a prominent feature of SMC proteins, and are thought to serve as spacer rods to provide an elongated structure and to separate domains. We reported recently that the coiled coils of mammalian condensin (SMC2/4) showed moderate sequence divergence (approximately 10-15%) consistent with their functioning as spacer rods. The coiled coils of mammalian cohesins (SMC1/3), however, were very highly constrained, with amino acid sequence divergence typically <0.5%. These coiled coils are among the most highly conserved mammalian proteins, suggesting that they make extensive contacts over their entire surface. METHODOLOGY/PRINCIPAL

findingsHere, we broaden our initial analysis of condensin and cohesin to include additional vertebrate and invertebrate organisms and multiple species of yeast. We found that the coiled coils of SMC1/3 are highly constrained in Drosophila and other insects, and more generally across all animal species. However, in yeast they are no more constrained than the coils of SMC2/4 and Ndc80/Nuf2p, suggesting that they are serving primarily as spacer rods. CONCLUSIONS/SIGNIFICANCE: SMC1/3 functions for sister chromatid cohesion in all species. Since its coiled coils apparently serve only as spacer rods in yeast, it is likely that this is sufficient for sister chromatid cohesion in all species. This suggests an additional function in animals that constrains the sequence of the coiled coils. Several recent studies have demonstrated that cohesin has a role in gene expression in post-mitotic neurons of Drosophila, and other animal cells. Some variants of human Cornelia de Lange Syndrome involve mutations in human SMC1/3. We suggest that the role of cohesin in gene expression may involve intimate contact of the coiled coils of SMC1/3, and impose the constraint on sequence divergence.

Indexed as

Conserved SequenceAdenosine TriphosphatasesAnimalsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsDNA-Binding ProteinsGene ExpressionHumansMultiprotein ComplexesProtein ConformationSpecies SpecificityStructural Homology, ProteinYeastsAdenosine TriphosphatasesCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinscondensin complexesDNA-Binding ProteinsMultiprotein Complexes

Identifiers

PMID19262687
PMCPMC2650401
OpenAlexW1991346963

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.