ArticlePloS one2013
Characterization of the interaction between the cohesin subunits Rad21 and SA1/2.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 47 citations in OpenAlex.
- Roles of meiotic and mitotic cohesin in stem cell gene regulation and genome stability.Molecular therapy. Nucleic acids · 2026Review
- StagX1, an isoquinolinone compound, selectively targets CES1-positive Ewing sarcoma cells as a potential therapeutic agent.Molecular therapy. Oncology · 2026Article
- Unfolded Protein Response as a Therapeutic Target: 4-(Heptyloxy)phenol Induces Programmed Cell Death in Ewing Sarcoma.Molecular cancer therapeutics · 2026Article
- STAG3 c.2776C > T, p.Arg926Ter is a recurrent variant in Russian patients with early-onset premature ovarian insufficiency.Journal of assisted reproduction and genetics · 2026Article
- Evolutionary Patterns of the Genes Involved in the Integrity and Segregation of Chromosomes in Sawflies (Hymenoptera: Symphyta).Ecology and evolution · 2026Article
- Substrate recognition by human separase.Science advances · 2025Article
- Comparative Phylogenetics Reveal Clade-specific Drivers of Recombination Rate Evolution Across Vertebrates.Molecular biology and evolution · 2025Article
- Co-essentiality analysis identifies PRR12 as a cohesin interacting protein and contributor to genomic integrity.Developmental cell · 2025Article
- Fdo1, Fkh1, Fkh2, and the Swi6-Mbp1 MBF complex regulate Mcd1 levels to impact eco1 rad61 cell growth in Saccharomyces cerevisiae.Genetics · 2024Article
- A non-canonical role of the inner kinetochore in regulating sister-chromatid cohesion at centromeres.The EMBO journal · 2024Article
- Role of chromosomal cohesion and separation in aneuploidy and tumorigenesis.Cellular and molecular life sciences : CMLS · 2024Review
- Loss of cohesin regulator PDS5A reveals repressive role of Polycomb loops.Nature communications · 2023Article
- An Updated Overview of the Role of CYP450 during Xenobiotic Metabolization in Regulating the Acute Myeloid Leukemia Microenvironment.International journal of molecular sciences · 2023Review
- Review
- It's all in the numbers: Cohesin stoichiometry.Frontiers in molecular biosciences · 2022Review
- Review
- Chromosome loading of cohesin depends on conserved residues in Scc3.Current genetics · 2021Article
- Cohesin subunit Rad21 binds to the HSV-1 genome near CTCF insulator sites during latencyJournal of virology · 2021Article
- Functional impact of cancer-associated cohesin variants on gene expression and cellular identity.Genetics · 2021Article
- Review
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
The cohesin complex is responsible for the fidelity of chromosomal segregation during mitosis. It consists of four core subunits, namely Rad21/Mcd1/Scc1, Smc1, Smc3, and one of the yeast Scc3 orthologs SA1 or SA2. Sister chromatid cohesion is generated during DNA replication and maintained until the onset of anaphase. Among the many proposed models of the cohesin complex, the 'core' cohesin subunits Smc1, Smc3, and Rad21 are almost universally displayed as tripartite ring. However, other than its supportive role in the cohesin ring, little is known about the fourth core subunit SA1/SA2. To gain deeper insight into the function of SA1/SA2 in the cohesin complex, we have mapped the interactive regions of SA2 and Rad21 in vitro and ex vivo. Whereas SA2 interacts with Rad21 through a broad region (301-750 aa), Rad21 binds to SA proteins through two SA-binding motifs on Rad21, namely N-terminal (NT) and middle part (MP) SA-binding motif, located at 60-81 aa of the N-terminus and 383-392 aa of the MP of Rad21, respectively. The MP SA-binding motif is a 10 amino acid, α-helical motif. Deletion of these 10 amino acids or mutation of three conserved amino acids (L(385), F(389), and T(390)) in this α-helical motif significantly hinders Rad21 from physically interacting with SA1/2. Besides the MP SA-binding motif, the NT SA-binding motif is also important for SA1/2 interaction. Although mutations on both SA-binding motifs disrupt Rad21-SA1/2 interaction, they had no apparent effect on the Smc1-Smc3-Rad21 interaction. However, the Rad21-Rad21 dimerization was reduced by the mutations, indicating potential involvement of the two SA-binding motifs in the formation of the two-ring handcuff for chromosomal cohesion. Furthermore, mutant Rad21 proteins failed to significantly rescue precocious chromosome separation caused by depletion of endogenous Rad21 in mitotic cells, further indicating the physiological significance of the two SA-binding motifs of Rad21.
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