%0 Journal Article
%T Interactions between the nuclear matrix proteins and the 5¡ä-flankingcis-acting elements of the human ¦Å-globin gene
%A Zhijiang Yan
%A Ruolan Qian
%J Chinese Science Bulletin
%@ 1861-9541
%D 1999
%I 
%R 10.1007/BF02885025
%X An erythroid-specific nuclear matrix protein (termed ¦Å-NMPk) in K562 cells, which can specifically bind to the positive stage-specific regulatory element (¦Å-PRE II, - 446 - 419 bp) upstream of the human ¦Å-globin gene, has been identified by using gel mobility shift assay. Meanwhile, Southwestern blotting assay showed that the nuclear matrix protein ¦Å-NMPk in K562, cells may be composed of two polypeptides (¡« 40 ku). In addition, it is observed in the gel mobility shift assay that the nuclear matrix proteins from K562, HEL and Raji cells can bind to the silencer DNA (- 392 - 177 bp) in the 5¡ä-flanking sequence of human ¦Å-globin gene respectively. However, the shift band K detected in K562 cells is different from shift band H/R in HEL and Raji cells, suggesting that a common nuclear matrix protein may exist in HEL and Raji cells. Results show that the nuclear matrix protein may play an important role in the regulation of the human ¦Å-globin gene expression.
%K human ¦Å-globin gene
%K cis-acting element
%K nuclear matrix protein
%U http://link.springer.com/article/10.1007/BF02885025