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1
Crystallization and preliminary diffraction analysis of human TEAD1, a transcriptional enhancer factor that controls the Hippo signaling pathway

Yeajin Mo,Hye Seon Lee,Chang Hoon Lee,Hwan Jung Lim,Seong Jun Park,Ho-Chul Shin,Seung Jun Kim,Bonsu Ku 한국구조생물학회 2018 Biodesign Vol.6 No.3
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Transcriptional enhancer activation domain (TEAD) proteins are transcription factors that promote the expression of genes involved in organogenesis, embryonic development, and tumorigenesis. TEAD functions downstream of the Hippo signaling pathway as one of the pivotal regulators that controls cell viability and proliferation, tissue growth, and organ size, by interacting with yes-associated protein (YAP) via its C-terminal YAP-binding domain (YBD). As YAP is a well-known oncoprotein and its interaction with TEAD has been shown to be critical for the function of YAP, TEAD proteins are emerging as a potential therapeutic target for cancer. In this study, the YBD of the TEAD1 protein was produced from an Escherichia coli expression system, purified using a Ni-NTA affinity chromatography, HiTrap Q anion exchange chromatography, and size exclusion chromatography, and then successfully crystallized. X-ray diffraction data were collected to the resolution of 1.70 Å. Preliminary diffraction analysis revealed that the TEAD1 YBD crystals belong to the space group P2 1 2 1 2 1 with unit cell parameters of a = 36.5 Å, b = 89.4 Å, c = 135.6 Å, and that two TEAD1 YBD molecules are contained in the asymmetric unit with a solvent content of 45.2%.
2
Structural and Biochemical Characterization of the Two Drosophila Low Molecular Weight-Protein Tyrosine Phosphatases DARP and Primo-1

Lee, Hye Seon,Mo, Yeajin,Shin, Ho-Chul,Kim, Seung Jun,Ku, Bonsu Korean Society for Molecular and Cellular Biology 2020 Molecules and cells Vol.43 No.12
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The Drosophila genome contains four low molecular weight-protein tyrosine phosphatase (LMW-PTP) members: Primo-1, Primo-2, CG14297, and CG31469. The lack of intensive biochemical analysis has limited our understanding of these proteins. Primo-1 and CG31469 were previously classified as pseudophosphatases, but CG31469 was also suggested to be a putative protein arginine phosphatase. Herein, we present the crystal structures of CG31469 and Primo-1, which are the first Drosophila LMW-PTP structures. Structural analysis showed that the two proteins adopt the typical LMW-PTP fold and have a canonically arranged P-loop. Intriguingly, while Primo-1 is presumed to be a canonical LMW-PTP, CG31469 is unique as it contains a threonine residue at the fifth position of the P-loop motif instead of highly conserved isoleucine and a characteristically narrow active site pocket, which should facilitate the accommodation of phosphoarginine. Subsequent biochemical analysis revealed that Primo-1 and CG31469 are enzymatically active on phosphotyrosine and phosphoarginine, respectively, refuting their classification as pseudophosphatases. Collectively, we provide structural and biochemical data on two Drosophila proteins: Primo-1, the canonical LMW-PTP protein, and CG31469, the first investigated eukaryotic protein arginine phosphatase. We named CG31469 as DARP, which stands for Drosophila ARginine Phosphatase.