The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer.

The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer.
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DOI:
10.1016/j.molcel.2014.01.010
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发表时间:
2014-02-06
期刊:
影响因子:
16
通讯作者:
Bai, Yawen
Bai, Yawen
中科院分区:
生物学1区
文献类型:
--
作者:
Hong, Jingjun;Feng, Hanqiao;Wang, Feng;Ranjan, Anand;Chen, Jianhong;Jiang, Jiansheng;Ghirlando, Rodolfo;Xiao, T. Sam;Wu, Carl;Bai, Yawen

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Histone variant H2A.Z-containing nucleosomes exist at most eukaryotic promoters and play important roles in gene transcription and genome stability. The multi-subunit nucleosome-remodeling enzyme complex SWR1, conserved from yeast to mammals, catalyzes the ATP-dependent replacement of histone H2A in canonical nucleosomes with H2A.Z. How SWR1 catalyzes the replacement reaction is largely unknown. Here we determined the crystal structure of the N-terminal region (599–627) of the catalytic subunit Swr1, termed Swr1-Z domain, in complex with the H2A.Z-H2B dimer at 1.78 Å resolution. The Swr1-Z domain forms a 310 helix and an irregular chain. A conserved LxxLF motif in the Swr1-Z 310 helix specifically recognizes the αC helix of H2A.Z. Our results show that the Swr1-Z domain can deliver the H2A.Z-H2B dimer to the DNA-(H3–H4)2 tetrasome to form the nucleosome by a histone chaperone mechanism.
DOI: 10.1038/msb.2008.25
发表时间: 2008
影响因子: 9.9
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发表时间: 1994-12-01
期刊: MOLECULAR AND GENERAL GENETICS
影响因子: --
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通讯作者: THOMAS, JO
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