Structure-function analysis of budding yeast cohesin complex involved in sister chromatid cohesion

粘着蛋白复合体参与保持复制的姐妹染色单体。姐妹染色单体凝聚力在真核生物中是保守的，并且是染色体忠实分离所必需的。Cohesin复合物由Smc蛋白和非Smc蛋白组成。然而，这种复合物的结构-功能关系仍然难以捉摸。我们已经使用高速原子力显微镜可视化的cohesin复合物。ATP酶结构域、卷曲螺旋区和二聚化结构域清晰可见。我们发现，这种结构域的组织是保守的其他Smc复合物和卷曲螺旋区的稳定性进行了观察。

Cohesin complex is involved in holding replicated sister chromatids. Sister chromatid cohesion is conserved among eukaryotes and is required for faithful segregation of chromosomes. Cohesin complex is comprised of Smc proteins and non-Smc proteins. However, the structure-function relationship of this complex remains elusive. We have used high speed atomic force microscopy to visualize the cohesin complex. We could clearly see ATPase domain, coiled coil region and dimerization domain. We found that this domain organization is conserved among other Smc complexes and the stability of coiled coil region was observed.