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Structural basis for the Rad6 activation by the Bre1 N-terminal domain

Meng Shi, Jiaqi Zhao, Mengfei Li, Wei Huang, Xue Bai, Wenxue Zhang, Kai Zhang, Xuefeng Chen, View ORCID ProfileSong Xiang
doi: https://doi.org/10.1101/2022.10.23.513400
Meng Shi
1Department of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), The province and ministry co-sponsored collaborative innovation center for medical epigenetics, Tianjin Medical University, Tianjin 300070, P. R. CHINA
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Jiaqi Zhao
1Department of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), The province and ministry co-sponsored collaborative innovation center for medical epigenetics, Tianjin Medical University, Tianjin 300070, P. R. CHINA
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Mengfei Li
2Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, TaiKang Center for Life and Medical Sciences, Frontier Science Centre of Immunology and Metabolism, Wuhan University, Wuhan 430072, P. R. CHINA
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Wei Huang
1Department of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), The province and ministry co-sponsored collaborative innovation center for medical epigenetics, Tianjin Medical University, Tianjin 300070, P. R. CHINA
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Xue Bai
1Department of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), The province and ministry co-sponsored collaborative innovation center for medical epigenetics, Tianjin Medical University, Tianjin 300070, P. R. CHINA
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Wenxue Zhang
3Department of Radiation Oncology, Tianjin Medical University General Hospital, Tianjin 300052, P. R. CHINA
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Kai Zhang
1Department of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), The province and ministry co-sponsored collaborative innovation center for medical epigenetics, Tianjin Medical University, Tianjin 300070, P. R. CHINA
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Xuefeng Chen
2Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, TaiKang Center for Life and Medical Sciences, Frontier Science Centre of Immunology and Metabolism, Wuhan University, Wuhan 430072, P. R. CHINA
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  • For correspondence: xfchen@whu.edu.cn xiangsong@tmu.edu.cn
Song Xiang
1Department of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), The province and ministry co-sponsored collaborative innovation center for medical epigenetics, Tianjin Medical University, Tianjin 300070, P. R. CHINA
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  • ORCID record for Song Xiang
  • For correspondence: xfchen@whu.edu.cn xiangsong@tmu.edu.cn
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Abstract

The mono-ubiquitination of the histone protein H2B (H2Bub1) is a highly conserved histone post-translational modification that plays critical roles in many fundamental processes. In yeast, this modification is catalyzed by the conserved Bre1-Rad6 complex. Bre1 contains a unique N-terminal Rad6 binding domain (RBD), how it interacts with Rad6 and contributes to the H2Bub1 catalysis is unclear. Here, we present crystal structure of the Bre1 RBD-Rad6 complex and structure-guided functional studies. Our structure provides a detailed picture of the interaction between the dimeric Bre1 RBD and a single Rad6 molecule. We further found that the interaction stimulates Rad6’s enzymatic activity by allosterically increasing its active site accessibility and likely contribute to the H2Bub1 catalysis through additional mechanisms. In line with these important functions, we found that the interaction is crucial for multiple H2Bub1-regulated processes. Our study provides molecular insights into the H2Bub1 catalysis.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted October 24, 2022.
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Structural basis for the Rad6 activation by the Bre1 N-terminal domain
Meng Shi, Jiaqi Zhao, Mengfei Li, Wei Huang, Xue Bai, Wenxue Zhang, Kai Zhang, Xuefeng Chen, Song Xiang
bioRxiv 2022.10.23.513400; doi: https://doi.org/10.1101/2022.10.23.513400
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Structural basis for the Rad6 activation by the Bre1 N-terminal domain
Meng Shi, Jiaqi Zhao, Mengfei Li, Wei Huang, Xue Bai, Wenxue Zhang, Kai Zhang, Xuefeng Chen, Song Xiang
bioRxiv 2022.10.23.513400; doi: https://doi.org/10.1101/2022.10.23.513400

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