Crystal Structure of the ULD (Ubiquitin Like Domain)-CUTL (CUT-repeat Like) Tandem of Special AT-rich Sequence Binding Protein 1 (SATB1) Reveals a Coordinating DNA-binding Mechanism [Gene Regulation]

August 14th, 2014 by Wang, Z., Yang, X., Guo, S., Yang, Y., Su, X.-C., Shen, Y., Long, J.

SATB1 is essential for T-cell development and growth and metastasis of multi-type 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 ULD and 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 binds 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 and HD (homeodomain) domains. These findings may reveal a multiple-domain-coordinated mechanism whereby SATB1 recognizes DNA targets.
  • Posted in Journal of Biological Chemistry, Publications
  • Comments Off on Crystal Structure of the ULD (Ubiquitin Like Domain)-CUTL (CUT-repeat Like) Tandem of Special AT-rich Sequence Binding Protein 1 (SATB1) Reveals a Coordinating DNA-binding Mechanism [Gene Regulation]