title: Crystal structure of the ubiquitin-like domain-CUT repeat-like tandem of special AT-rich sequence binding protein 1 (SATB1) reveals a coordinating DNA-binding mechanism.
abstract: SATB1 is essential for T-cell development and growth and metastasis of multitype tumors and acts as a global chromatin organizer and gene expression regulator. The DNA binding ability of SATB1 plays vital roles in its various biological functions. We report the crystal structure of the N-terminal module of SATB1. Interestingly, this module contains a ubiquitin-like domain (ULD) and a CUT repeat-like (CUTL) domain (ULD-CUTL tandem). Detailed biochemical experiments indicate that the N terminus of SATB1 (residues 1-248, SATB1((1-248))), including the extreme 70 N-terminal amino acids, and the ULD-CUTL tandem bind specifically to DNA targets. Our results show that the DNA binding ability of full-length SATB1 requires the contribution of the CUTL domain, as well as the CUT1-CUT2 tandem domain and the homeodomain. These findings may reveal a multiple-domain-coordinated mechanism whereby SATB1 recognizes DNA targets.
authors.affiliation: From the State Key Laboratory of Medicinal Chemical Biology, the College of Life Sciences, and.
authors.forename: Zheng
authors.initials: Z
authors.lastname: Wang
authors.affiliation: From the State Key Laboratory of Medicinal Chemical Biology, the College of Life Sciences, and.
authors.forename: Xue
authors.initials: X
authors.lastname: Yang
authors.affiliation: From the State Key Laboratory of Medicinal Chemical Biology.
authors.forename: Shuang
authors.initials: S
authors.lastname: Guo
authors.affiliation: the State Key Laboratory of Elemento-organic Chemistry, Nankai University and.
authors.forename: Yin
authors.initials: Y
authors.lastname: Yang
authors.affiliation: the State Key Laboratory of Elemento-organic Chemistry, Nankai University and.
authors.forename: Xun-Cheng
authors.initials: XC
authors.lastname: Su
authors.affiliation: From the State Key Laboratory of Medicinal Chemical Biology, the College of Life Sciences, and the Synergetic Innovation Center of Chemical Science and Engineering, Tianjin 300071, China shenyuequan@gmail.com.
authors.forename: Yuequan
authors.initials: Y
authors.lastname: Shen
authors.affiliation: From the State Key Laboratory of Medicinal Chemical Biology, the College of Life Sciences, and jflong@nankai.edu.cn.
authors.forename: Jiafu
authors.initials: J
authors.lastname: Long
mesh_terms: D020856:AT Rich Sequence; D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D036961:Matrix Attachment Region Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D025801:Ubiquitin
chemical_list: D004268:DNA-Binding Proteins; D036961:Matrix Attachment Region Binding Proteins; C469541:Satb1 protein, mouse; D025801:Ubiquitin; D004247:DNA
keywords: CUTL Domain; Chromatin Regulation; Coordination Mechanism; Crystal Structure; DNA Binding; DNA-binding Protein; Gene Regulation; Global Gene Regulation; SATB1; Scaffold Protein