Evidence map›Paper›PMID 25748820›Full record

ArticlePLoS genetics2015

A conserved domain in the scc3 subunit of cohesin mediates the interaction with both mcd1 and the cohesin loader complex.

Ola Orgil, Avi Matityahu, Thomas Eng, Vincent Guacci, Douglas Koshland, Itay Onn

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

41 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  3. Aberrant cohesin function inbioRxiv : the preprint server for biology · 2025
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  4. NIPBL and STAG1 enable loop extrusion by providing differential DNA-cohesin affinity.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

6 authors at 2 institutions in 2 countries.

Ola OrgilFaculty of Medicine in The Galilee, Bar-Ilan University, Safed, Israel.
Avi MatityahuFaculty of Medicine in The Galilee, Bar-Ilan University, Safed, Israel.
Thomas EngDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, United States of America.
Vincent GuacciDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, United States of America.
Douglas KoshlandDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, United States of America.
Itay OnnFaculty of Medicine in The Galilee, Bar-Ilan University, Safed, Israel.
Bar-Ilan University · ILUniversity of California, Berkeley · US

Funding

Establishment of sister chromatid cohesionR01GM092813 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KOSHLAND, DOUGLAS E · 2010 to 2015
$2.2M
NIGMS NIH HHS GM092813NIGMS NIH HHS R01 GM092813
6 · The paper itself

Abstract

The Structural Maintenance of Chromosome (SMC) complex, termed cohesin, is essential for sister chromatid cohesion. Cohesin is also important for chromosome condensation, DNA repair, and gene expression. Cohesin is comprised of Scc3, Mcd1, Smc1, and Smc3. Scc3 also binds Pds5 and Wpl1, cohesin-associated proteins that regulate cohesin function, and to the Scc2/4 cohesin loader. We mutagenized SCC3 to elucidate its role in cohesin function. A 5 amino acid insertion after Scc3 residue I358, or a missense mutation of residue D373 in the adjacent stromalin conservative domain (SCD) induce inviability and defects in both cohesion and cohesin binding to chromosomes. The I358 and D373 mutants abrogate Scc3 binding to Mcd1. These results define an Scc3 region extending from I358 through the SCD required for binding Mcd1, cohesin localization to chromosomes and cohesion. Scc3 binding to the cohesin loader, Pds5 and Wpl1 are unaffected in I358 mutant and the loader still binds the cohesin core trimer (Mcd1, Smc1 and Smc3). Thus, Scc3 plays a critical role in cohesin binding to chromosomes and cohesion at a step distinct from loader binding to the cohesin trimer. We show that residues Y371 and K372 within the SCD are critical for viability and chromosome condensation but dispensable for cohesion. However, scc3 Y371A and scc3 K372A bind normally to Mcd1. These alleles also provide evidence that Scc3 has distinct mechanisms of cohesin loading to different loci. The cohesion-competence, condensation-incompetence of Y371 and K372 mutants suggests that cohesin has at least one activity required specifically for condensation.

Indexed as

Cell Cycle ProteinsCell NucleusChromatidsChromosomal Proteins, Non-HistoneChromosome SegregationChromosomes, FungalCohesinsDNA RepairMutationNuclear ProteinsProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsIRR1 protein, S cerevisiaeMCD1 protein, S cerevisiaeNuclear ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID25748820
PMCPMC4352044
OpenAlexW1973752471

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.