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Volume 28, No 11, Nov 2018

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 28 Issue 11, November 2018: 1121-1123

LETTERS TO THE EDITOR

Cryo-EM structure of human SRCAP complex

Yangyang Feng 1, Yuan Tian 1, Zihan Wu 1 and Yanhui Xu 1,2,3,4

1Fudan University Shanghai Cancer Center, Key Laboratory of Medical Epigenetics and Metabolism, Institute of Biomedical Sciences,Shanghai Medical College of Fudan University, Shanghai 200032,China; 2Key Laboratory of Molecular Medicine, Ministry of Education,Department of Systems Biology for Medicine, School of Basic Medical Sciences, Shanghai Medical College of Fudan University, Shanghai 200032, China; 3State Key Laboratory of Genetic Engineering,Collaborative Innovation Center of Genetics and Development,School of Life Sciences, Fudan University, Shanghai 200433, China and 4CAS Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai 200031, China
 Correspondence: These authors contributed equally: Yangyang Feng, Yuan TianCorrespondence: Yanhui Xu (xuyh@fudan.edu.cn)

Dear Editor,

Eukaryotic genome packs into highly condensed chromatin, in which genomic DNA wraps around histone octamer formed by evolutionarily conserved histone proteins H2A, H2B, H3, and H4. The histone variant H2A.Z primarily exists within nucleosomes that flank gene promoters, centromeres, and chromatin boundaries. The H2A.Z-containing nucleosomes undergo rapid turnover, which is important for the regulation of gene expression, DNA repair, and chromosome stability1. The deposition of H2A.Z into genome is uniquely dependent on the SWI/SNF (switch/sucrose non-fermentable)-related Swr1 complex (referred to as Swr1-C hereafter) in yeast and SNF2-Related CBP Activator Protein (SRCAP) complex (referred to as SRCAP-C hereafter) in human. Swr1-C/SRCAP-C incorporates H2A.Z/H2B dimer into canonical nucleosomes coupled with the eviction of H2A/H2B dimer in a stepwise exchange manner2,3,4.


https://doi.org/10.1038/s41422-018-0102-y

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