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| Content Provider | Springer Nature Link |
|---|---|
| Author | Hou, Chunhui Huang, Jian Zhang, Shubing Qian, Ruolan |
| Copyright Year | 2002 |
| Abstract | 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. |
| Starting Page | 1543 |
| Ending Page | 1546 |
| Page Count | 4 |
| File Format | |
| ISSN | 10016538 |
| Journal | Chinese Science Bulletin |
| Volume Number | 47 |
| Issue Number | 18 |
| e-ISSN | 18619541 |
| Language | English |
| Publisher | Science in China Press |
| Publisher Date | 2002-01-01 |
| Publisher Place | Beijing |
| Access Restriction | Subscribed |
| Subject Keyword | HMG proteins human ε-globin gene promoter in vitro nucleosome reconstitution HMG proteins purification EMSA Science Life Sciences Physics Chemistry/Food Science Earth Sciences Engineering |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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