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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.

SUBMITTER: Wang Z

PROVIDER: S-EPMC3351170 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

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The structural basis for the oligomerization of the N-terminal domain of SATB1.

Wang Zheng Z Yang Xue X Chu Xinlei X Zhang Jinxiu J Zhou Hao H Shen Yuequan Y Long Jiafu J

Nucleic acids research 20120112 9

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 ...[more]

PMID: 22241778

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