Post-translational modifications play important roles in mediating protein functions in a wide variety of cellular events in vivo. HEMK2–TRMT112 heterodimer has been reported to be responsible for both histone lysine methylation and eukaryotic release factor 1 (eRF1) glutamine methylation. However, how HEMK2–TRMT112 complex recognizes and catalyzes eRF1 glutamine methylation is largely unknown. Here, we present two structures of HEMK2–TRMT112, with one bound to SAM and the other bound with SAH and methylglutamine (Qme). Structural analyses of the post-catalytic complex, complemented by mass spectrometry experiments, indicate that the HEMK2 utilizes a specific pocket to accommodate the substrate glutamine and catalyzes the subsequent methylation. Therefore, our work not only throws light on the protein glutamine methylation mechanism, but also reveals the dual activity of HEMK2 by catalyzing the methylation of both Lys and Gln residues.
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October 2020
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Cover Image
The cover image showing the crystal structure of human hemoglobin (PDB: 1GZX). For more information, see the article by Natarajan et al. (pp. 3839–3850). Artwork Image courtesy of C. Natarajan.
Research Article|
October 12 2020
Structural insight into HEMK2–TRMT112-mediated glutamine methylation
Jie Gao
;
Jie Gao
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, P. R. China
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Bin Wang;
Bin Wang
2Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, No. 152 Luoyu Road, Wuhan 430079, P. R. China
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Huijuan Yu;
Huijuan Yu
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, P. R. China
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Gao Wu;
Gao Wu
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, P. R. China
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Cuihong Wan;
Cuihong Wan
2Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, No. 152 Luoyu Road, Wuhan 430079, P. R. China
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Wenting Liu;
Wenting Liu
3Hefei HanKeMab, Biotechnology Co., Hefei 230088, P. R. China
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Shanhui Liao;
Shanhui Liao
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, P. R. China
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Liansheng Cheng;
3Hefei HanKeMab, Biotechnology Co., Hefei 230088, P. R. China
Correspondence: Liansheng Cheng (charlson@ustc.edu.cn) or Zhongliang Zhu (zlzhu63@ustc.edu.cn)
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Zhongliang Zhu
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, P. R. China
Correspondence: Liansheng Cheng (charlson@ustc.edu.cn) or Zhongliang Zhu (zlzhu63@ustc.edu.cn)
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Publisher: Portland Press Ltd
Received:
July 30 2020
Revision Received:
September 09 2020
Accepted:
September 24 2020
Accepted Manuscript online:
September 24 2020
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2020
Biochem J (2020) 477 (19): 3833–3838.
Article history
Received:
July 30 2020
Revision Received:
September 09 2020
Accepted:
September 24 2020
Accepted Manuscript online:
September 24 2020
Citation
Jie Gao, Bin Wang, Huijuan Yu, Gao Wu, Cuihong Wan, Wenting Liu, Shanhui Liao, Liansheng Cheng, Zhongliang Zhu; Structural insight into HEMK2–TRMT112-mediated glutamine methylation. Biochem J 16 October 2020; 477 (19): 3833–3838. doi: https://doi.org/10.1042/BCJ20200594
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