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A handcuff model for the cohesin complex
- Source :
- The Journal of Cell Biology
- Publication Year :
- 2008
- Publisher :
- Rockefeller University Press, 2008.
-
Abstract
- The cohesin complex is responsible for the accurate separation of sister chromatids into two daughter cells. Several models for the cohesin complex have been proposed, but the one-ring embrace model currently predominates the field. However, the static configuration of the embrace model is not flexible enough for cohesins to perform their functions during DNA replication, transcription, and DNA repair. We used coimmunoprecipitation, a protein fragment complement assay, and a yeast two-hybrid assay to analyze the protein–protein interactions among cohesin subunits. The results show that three of the four human cohesin core subunits (Smc1, Smc3, and Rad21) interact with themselves in an Scc3 (SA1/SA2)-dependent manner. These data support a two-ring handcuff model for the cohesin complex, which is flexible enough to establish and maintain sister chromatid cohesion as well as ensure the fidelity of chromosome segregation in higher eukaryotes.
- Subjects :
- Cohesin complex
Chromosomal Proteins, Non-Histone
DNA repair
Blotting, Western
Cell Cycle Proteins
Chromatids
Biology
Models, Biological
Article
Chromosome segregation
03 medical and health sciences
0302 clinical medicine
Two-Hybrid System Techniques
Humans
Immunoprecipitation
Sister chromatids
Research Articles
030304 developmental biology
Genetics
0303 health sciences
Cohesin
Genetic Complementation Test
DNA replication
Nuclear Proteins
Cell Biology
Phosphoproteins
Cell biology
DNA-Binding Proteins
Establishment of sister chromatid cohesion
Luminescent Proteins
Protein Subunits
Multiprotein Complexes
Chromatid
biological phenomena, cell phenomena, and immunity
030217 neurology & neurosurgery
HeLa Cells
Protein Binding
Subjects
Details
- ISSN :
- 15408140 and 00219525
- Volume :
- 183
- Database :
- OpenAIRE
- Journal :
- Journal of Cell Biology
- Accession number :
- edsair.doi.dedup.....ab3c46b29cf2ae3e6dbbf3db2cfe18ee
- Full Text :
- https://doi.org/10.1083/jcb.200801157