Distinct and overlapping roles of STAG1 and STAG2 in cohesin localization and gene expression in embryonic stem cells [ChIP-seq]

Purpose: Cohesin is a ring-shaped complex that is critical to genome organization and is an important regulator of gene expression. How cohesin accessory proteins contribute to cohesin function remains unclear. The purpose of this study is to assess the roles of cohesin accessory proteins, STAG1 and STAG2, in cohesin localization and gene expression. Method: Genome wide binding patterns of the STAGs and cohesin in wildtype cells as well as in STAG CRISPR/Cas9 genome edited knockout cells were assessed via chromatin immunoprecipitation followed by high throughput sequencing (ChIP-seq). The redundancy of the STAGs was addressed by using siRNA against STAG1 in a STAG2-knockout background. Overall design: ChIP-seq was performed in wildtype mESCs in duplicate for STAG1, STAG2 and RAD21. ChIP-seq was performed in CRISPR-Cas9 genome edited STAG deletion mESCs in duplicate for the reciprocal STAG and RAD21. ChIP-seq was performed in wildtype and Stag2-KO cells after being treated with either siGLO transfection control or siStag1. Please note that each processed data was generated from both replicates and is linked to the corresponding *Rep1 sample records.