Yeast Hif1 [Hat1 (histone acetyltransferase 1)-interacting factor], a homologue of human NASP (nuclear autoantigenic sperm protein), is a histone chaperone that is involved in various protein complexes which modify histones during telomeric silencing and chromatin reassembly. For elucidating the structural basis of Hif1, in the present paper we demonstrate the crystal structure of Hif1 consisting of a superhelixed TPR (tetratricopeptide repeat) domain and an extended acid loop covering the rear of TPR domain, which represent typical characteristics of SHNi-TPR [Sim3 (start independent of mitosis 3)-Hif1-NASP interrupted TPR] proteins. Our binding assay indicates that Hif1 could bind to the histone octamer via histones H3 and H4. The acid loop is shown to be crucial for the binding of histones and may also change the conformation of the TPR groove. By binding to the core histone complex Hif1 may recruit functional protein complexes to modify histones during chromatin reassembly.
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September 2014
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Research Article|
August 22 2014
Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones
Hejun Liu;
Hejun Liu
1
*Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China
†Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui, 230026, People's Republic of China
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Mengying Zhang;
Mengying Zhang
1
*Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China
†Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui, 230026, People's Republic of China
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Wei He;
Wei He
*Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China
†Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui, 230026, People's Republic of China
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Zhongliang Zhu;
Zhongliang Zhu
*Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China
†Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui, 230026, People's Republic of China
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Maikun Teng;
Maikun Teng
*Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China
†Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui, 230026, People's Republic of China
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Yongxiang Gao;
Yongxiang Gao
2
*Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China
†Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui, 230026, People's Republic of China
2Correspondence may be addressed to either of these authors (email [email protected] or [email protected]).
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Liwen Niu
Liwen Niu
2
*Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China
†Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui, 230026, People's Republic of China
2Correspondence may be addressed to either of these authors (email [email protected] or [email protected]).
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Publisher: Portland Press Ltd
Received:
December 13 2013
Revision Received:
May 26 2014
Accepted:
June 20 2014
Accepted Manuscript online:
June 20 2014
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2014 Biochemical Society
2014
Biochem J (2014) 462 (3): 465–473.
Article history
Received:
December 13 2013
Revision Received:
May 26 2014
Accepted:
June 20 2014
Accepted Manuscript online:
June 20 2014
Citation
Hejun Liu, Mengying Zhang, Wei He, Zhongliang Zhu, Maikun Teng, Yongxiang Gao, Liwen Niu; Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones. Biochem J 15 September 2014; 462 (3): 465–473. doi: https://doi.org/10.1042/BJ20131640
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