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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, thebinding of HMG proteins (HMG1/2 and HMG14/17) to the human ε-globin gene promoter (ε-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 ε-promoter DNA, however, HMG14/17 could not. Using the in vitro nucleosome recons- titution, we revealed that HMG14/17 could bind to the mononucleosome reconstituted in vitro with ε-promoter,whi- le HMG1/2 could not. Those results indicate that the binding of HMG proteins to ε-promoter is dynamic as the nucleo- some assembling and disassembling. Wespeculated that this selective binding of HMG proteins to ε-promoter might playa critical role in the regulation of ε-globin gene expression.