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

Xiuna Yang; Masahiro Morita; Hui Wang; Toru Suzuki; Wen Yang; Yunhai Luo; Cong Zhao; Yue Yu; Mark Bartlam; Tadashi Yamamoto; Zihe Rao

doi:10.1093/nar/gkn825

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

Xiuna Yang, Masahiro Morita, Hui Wang, Toru Suzuki, Wen Yang, Yunhai Luo, Cong Zhao, Yue Yu, Mark Bartlam, Tadashi Yamamoto, Zihe Rao

Research output: Contribution to journal › Article › peer-review

39 Scopus citations

Abstract

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 2.3Å and 2.2Å 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.

Original language	English (US)
Pages (from-to)	6872-6881
Number of pages	10
Journal	Nucleic acids research
Volume	36
Issue number	21
DOIs	https://doi.org/10.1093/nar/gkn825
State	Published - 2008
Externally published	Yes

ASJC Scopus subject areas

Genetics

Access to Document

10.1093/nar/gkn825

Cite this

@article{b6e11aec586e4e76b402a8fc741b617a,

title = "Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity",

abstract = "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{\AA} and 2.2{\AA} 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.",

author = "Xiuna Yang and Masahiro Morita and Hui Wang and Toru Suzuki and Wen Yang and Yunhai Luo and Cong Zhao and Yue Yu and Mark Bartlam and Tadashi Yamamoto and Zihe Rao",

note = "Funding Information: The Ministry of Science and Technology International Cooperation Project (grant number 2006DFB32420); the Ministry of Science and Technology 973 Project (grant number 2007CB914301); the National Natural Science Foundation of China (grant numbers 30221003 and 30770438); the Global COE Program (Integrative Life Science Based on the Study of Biosignaling Mechanisms partial), MEXT, Japan. Funding for open access charge: Ministry of Science and Technology of China.",

year = "2008",

doi = "10.1093/nar/gkn825",

language = "English (US)",

volume = "36",

pages = "6872--6881",

journal = "Nucleic acids research",

issn = "0305-1048",

publisher = "Oxford University Press",

number = "21",

}

TY - JOUR

T1 - Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity

AU - Yang, Xiuna

AU - Morita, Masahiro

AU - Wang, Hui

AU - Suzuki, Toru

AU - Yang, Wen

AU - Luo, Yunhai

AU - Zhao, Cong

AU - Yu, Yue

AU - Bartlam, Mark

AU - Yamamoto, Tadashi

AU - Rao, Zihe

N1 - Funding Information: The Ministry of Science and Technology International Cooperation Project (grant number 2006DFB32420); the Ministry of Science and Technology 973 Project (grant number 2007CB914301); the National Natural Science Foundation of China (grant numbers 30221003 and 30770438); the Global COE Program (Integrative Life Science Based on the Study of Biosignaling Mechanisms partial), MEXT, Japan. Funding for open access charge: Ministry of Science and Technology of China.

PY - 2008

Y1 - 2008

N2 - 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 2.3Å and 2.2Å 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.

AB - 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 2.3Å and 2.2Å 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.

UR - http://www.scopus.com/inward/record.url?scp=57149102295&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=57149102295&partnerID=8YFLogxK

U2 - 10.1093/nar/gkn825

DO - 10.1093/nar/gkn825

M3 - Article

C2 - 18974182

AN - SCOPUS:57149102295

SN - 0305-1048

VL - 36

SP - 6872

EP - 6881

JO - Nucleic acids research

JF - Nucleic acids research

IS - 21

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this