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Nucleic Acids Research Advance Access originally published online on October 30, 2008
Nucleic Acids Research 2008 36(21):6872-6881; doi:10.1093/nar/gkn825
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Nucleic Acids Research, 2008, Vol. 36, No. 21 6872-6881
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity

Xiuna Yang1,2, Masahiro Morita3, Hui Wang1,2, Toru Suzuki3, Wen Yang1,4, Yunhai Luo1, Cong Zhao4, Yue Yu5, Mark Bartlam4, Tadashi Yamamoto3,* and Zihe Rao1,2,4

1Laboratory of Structural Biology, Tsinghua University, Beijing 100084, 2National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China, 3Division of Oncology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan, 4College of Life Sciences & Tianjin State Laboratory of Protein Sciences, Nankai University, Tianjin 300071 and 5Shenzhen College of International Education, Shenzhen 518048, China

*To whom correspondence should be addressed. Tel: +81 3 5449 5301; Fax: +81 3 5449 5413; Email: tyamamot{at}ims.u-tokyo.ac.jp

Correspondence may also be addressed to Mark Bartlam. Tel: +86 22 2350 2351; Fax: +86 22 2350 2351; Email: bartlam{at}nankai.edu.cn

Received May 5, 2008. Revised October 13, 2008. Accepted October 14, 2008.

BTG2 is the prototypical member of the TOB family and is known to be involved in cell growth, differentiation and DNA repair. As a transcriptional co-regulator, BTG2 interacts with CCR4-associated factor 1 (CAF1) and POP2 (CALIF), which are key components of the general CCR4/NOT multi-subunit transcription complex, and which are reported to play distinct roles as nucleases involved in mRNA deadenylation. Here we report the crystal structures of human BTG2 and mouse TIS21 to 2.3 Å and 2.2 Å resolution, respectively. The structures reveal the putative CAF1 binding site. CAF1 deadenylase assays were performed with wild-type BTG2 and mutants that disrupt the interaction with CAF1. The results reveal the suppressive role of BTG2 in the regulation of CAF1 deadenylase activity. Our study provides insights into the formation of the BTG2-CAF1 complex and the potential role of BTG2 in the regulation of CAF1.


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