Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the human TLE1 Q domain.

Abstract

Human transducin-like enhancer of split 1 (TLE1) plays crucial roles in a number of developmental processes and is involved in pathogenesis of malignancy tumors. The N-terminal glutamine-rich domain (Q domain) of TLE1 mediates its tetramerization and interactions with different DNA-binding transcription factors to regulate Notch and Wnt signaling pathways. To better understand the molecular mechanism of TLE1's functions in these pathways, we cloned, purified, and crystallized the TLE1 Q domain (TLE1-Q). The crystals belong to space group C222(1), with the complete diffraction data of the native and Se-Met TLE1-Q collected to 3.5 and 4.1 Å resolutions, respectively. The phasing-solving and model building are in progress.

• Authors: Su Wang, Jiamu Du, Hua Tang, Xinyu Ding, Manwu Zha, Zhifei Xu
• Journal: Acta biochimica et biophysica Sinica (Acta Biochim Biophys Sin (Shanghai)) Vol. 43 Issue 2 Pg. 149-53 (Feb 2011) ISSN: 1745-7270 [Electronic] China
• PMID: 21183761 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Co-Repressor Proteins
• Repressor Proteins
• TLE1 protein, human

Topics

• Circular Dichroism (instrumentation)
• Cloning, Molecular (methods)
• Co-Repressor Proteins
• Crystallization (methods)
• Humans
• Repressor Proteins (biosynthesis, genetics, isolation & purification)
• X-Ray Diffraction (methods)