title: The structural basis for the oligomerization of the N-terminal domain of SATB1.
abstract: Special AT-rich sequence-binding protein 1 (SATB1) is a global chromatin organizer and gene expression regulator essential for T-cell development and breast cancer tumor growth and metastasis. The oligomerization of the N-terminal domain of SATB1 is critical for its biological function. We determined the crystal structure of the N-terminal domain of SATB1. Surprisingly, this domain resembles a ubiquitin domain instead of the previously proposed PDZ domain. Our results also reveal that SATB1 can form a tetramer through its N-terminal domain. The tetramerization of SATB1 plays an essential role in its binding to highly specialized DNA sequences. Furthermore, isothermal titration calorimetry results indicate that the SATB1 tetramer can bind simultaneously to two DNA targets. Based on these results, we propose a molecular model whereby SATB1 regulates the expression of multiple genes both locally and at a distance.
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology and College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
authors.forename: Zheng
authors.initials: Z
authors.lastname: Wang
authors.forename: Xue
authors.initials: X
authors.lastname: Yang
authors.forename: Xinlei
authors.initials: X
authors.lastname: Chu
authors.forename: Jinxiu
authors.initials: J
authors.lastname: Zhang
authors.forename: Hao
authors.initials: H
authors.lastname: Zhou
authors.forename: Yuequan
authors.initials: Y
authors.lastname: Shen
authors.forename: Jiafu
authors.initials: J
authors.lastname: Long
mesh_terms: D004247:DNA / Q000378:metabolism; D036961:Matrix Attachment Region Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary
chemical_list: D036961:Matrix Attachment Region Binding Proteins; C469541:Satb1 protein, mouse; D004247:DNA