Interactions between HMG proteins (HMG1/2 and HMG14/17) and human ε-globin gene promoter (ε-promoter)  

作　　者：Chunhui Hou Jian Huang Shubing Zhang Ruolan Qian 

出　　处：《Chinese Science Bulletin》2002年第18期1543-1546,共4页

基　　金：This work was supported by the National Natural Science Foundation of China (Grant No. 39893320);the Foundation of Chinese Academy of Sciences (Grant No. KJ 951 -A 1 -603 (2)).

摘　　要：High mobility group (HMG) proteins are abundant non-histone proteins in the nuclei of eukaryocytes. It has been shown that HMG proteins may play important roles in the structure and function of chromatin. In the present study, the binding of HMG proteins (HMG1/2 and HMG14/17) to the human e-globin gene promoter (e-promo-ter, -177-+1 bp) has been examined by using both the in vitro nucleosome reconstitution and the electrophoresis mobility shift assay (EMSA). We found that HMG1/2 proteins could bind to the naked e-promoter DNA, however, HMG14/17 could not. Using the in vitro nucleosome reconstitution, we revealed that HMG14/17 could bind to the mononucleosome reconstituted in vitro with E-promoter, while HMG1/2 could not. Those results indicate that the binding of HMG proteins to e-promoter is dynamic as the nucleosome assembling and disassembling. We speculated that this selective binding of HMG proteins to e-promoter might play a critical role in the regulation of e-globin gene expression.High mobility group (HMG) proteins are abundant non-histone proteins in the nuclei of eukaryocytes. It has been shown that HMG proteins may play important roles in the structure and function of chromatin. In the present study, the binding of HMG proteins (HMG1/2 and HMG14/17) to the human ε-globin gene promoter (ε-promoter, ?177–+1 bp) has been examined by using both the in vitro nucleosome reconstitution and the electrophoresis mobility shift assay (EMSA). We found that HMG1/2 proteins could bind to the naked ε-promoter DNA, however, HMG14/17 could not. Using the in vitro nucleosome reconstitution, we revealed that HMG14/17 could bind to the mononucleosome reconstituted in vitro with ε-promoter, while HMG1/2 could not. Those results indicate that the binding of HMG proteins to ε-promoter is dynamic as the nucleosome assembling and disassembling. We speculated that this selective binding of HMG proteins to ε-promoter might play a critical role in the regulation of ε-globin gene expression.

关 键 词：HMG PROTEINS HUMAN ε-globin gene PROMOTER in vitro NUCLEOSOME reconstitution HMG PROTEINS purification EMSA. 

分 类 号：Q753[生物学—分子生物学]