| Literature DB >> 26974124 |
Xiaoping Liang1,2, Shan Shan1, Lu Pan1,2, Jicheng Zhao1, Anand Ranjan3, Feng Wang4, Zhuqiang Zhang1, Yingzi Huang1, Hanqiao Feng4, Debbie Wei4, Li Huang1,2, Xuehui Liu1, Qiang Zhong1, Jizhong Lou1, Guohong Li1, Carl Wu3,4, Zheng Zhou1,2.
Abstract
Histone variant H2A.Z, a universal mark of dynamic nucleosomes flanking gene promoters and enhancers, is incorporated into chromatin by SRCAP (SWR1), an ATP-dependent, multicomponent chromatin-remodeling complex. The YL1 (Swc2) subunit of SRCAP (SWR1) plays an essential role in H2A.Z recognition, but how it achieves this has been unclear. Here, we report the crystal structure of the H2A.Z-binding domain of Drosophila melanogaster YL1 (dYL1-Z) in complex with an H2A.Z-H2B dimer at 1.9-Å resolution. The dYL1-Z domain adopts a new whip-like structure that wraps over H2A.Z-H2B, and preferential recognition is largely conferred by three residues in loop 2, the hyperacidic patch and the extended αC helix of H2A.Z. Importantly, this domain is essential for deposition of budding yeast H2A.Z in vivo and SRCAP (SWR1)-catalyzed histone H2A.Z replacement in vitro. Our studies distinguish YL1-Z from known H2A.Z chaperones and suggest a hierarchical mechanism based on increasing binding affinity facilitating H2A.Z transfer from SRCAP (SWR1) to the nucleosome.Entities:
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Year: 2016 PMID： 26974124 DOI： 10.1038/nsmb.3190
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN： 1545-9985 Impact factor: 15.369