Genome-wide identification of histone H2A and histone variant H2A.Z-interacting proteins by bPPI-seq  

作　　者：Yi Zhang Wai Lim Ku Shuai Liu Kairong Cui Wenfei Jin Qingsong Tarlg William Lu Bing Ni Keji Zhao 

机构地区：[1]Institute of Immunology PLA, Third Military Medical University, Chongqing 400038, China [2]Systems Biology Center, Division of Intramural Research, NHLBI, NIH, Bethesda, AID 20892, USA [3]Department of Pathophysiology and High Altitude Pathology,Third Military Medical University, Chongqing 400038, China

出　　处：《Cell Research》2017年第10期1258-1274,共17页细胞研究（英文版）

摘　　要：H2A is a nucleosome core subunit involved in organizing DNA into a chromatin structure that is often inacces- sible to regulatory enzymes. Replacement of H2A by its variant H2A.Z renders chromatin accessible at enhancers and promoters. However, it remains unclear how H2A.Z functions so differently from canonical H2A. Here we report the genome-wide identification of proteins that directly interact with H2A and H2A.Z in vivo using a novel strategy, bPPI-seq. We show that bPPI-seq is a sensitive and robust technique to identify protein-protein interactions in vivo. Our data indicate that H2A.Z-interacting proteins and H2A-interaeting proteins participate in distinct bio- logical processes. In contrast to H2A-interacting proteins, the H2A.Z-interacting proteins are involved in transcrip- tional regulation. We found that the transcription factor Osrl interacts with H2A.Z both in vitro and in vivo. It also mediates H2A.Z incorporation to a large number of target sites and regulates gene expression. Our data indicate that bPPI-seq can be widely applied to identify genome-wide interacting proteins under physiological conditions.

关 键 词：bPPI-seq protein-protein interactions H2A H2A.Z Osrl 

分 类 号：Q78[生物学—分子生物学] V475.1[航空宇航科学与技术—飞行器设计]