Hsp90�� Gene Distal Dnasei-sensitive Sites And Its 5 'shanghai Distal Genomic Fragment Functions Preliminary Study

HSP90 is an important member of HSP protein family. HSP90 usually constitutively expressed in most mammalian cell types and can be further induced by heat shock and other stresses. HSP90 proteins are molecular chaperones that associated with cellar signal transduction, steroid hormone response, and cell cycle regulation, they are critical to the survival of cell in the normal and pathological conditions. So it is very meaningful for us to study the regulatory mechanisms of human hsp90 genes.The regulation and expression mechanism of hsp90 gene is so intricate, It include the changes in chromatin structure, activation of the special transcription factor of HSF, the increasing stability of heat shock protein mRNA and the control of finite translation. When the activated heat shock factors bind to heat shock protein, feedback check decrease its activity, to get to the balance between the HSP90 expression and the out world circumstances. It is such a fine process that we can't image. It would be a good regulatory model of the eukaryotic gene expression when its mechanism was complete elucidated. There are many members in heat shock protein family, but they have some common characters in the regulation of gene. Heat shock proteins occupy an important feature that is their conservation. The promoter region of hsp genes often contain the binding sequences of a series trans-factors which induce the basic transcription, such as SP1, CAAT and ATF, and with some heat shock elements in their 5' upstream. HSP exert its function with these cis-elements in normal and stress condition.Carl Wu first found a series of DNasel hypersensitive sites in Drosophila hsp70 gene when he tried studying the chromatin structure and the gene transcription regulation in chromatin in 1980. Michael A studied the 5' DNasel hypersensitive sites of Drosophila hsp22, hsp23, hsp26, hsp28 locus. Kullum and Schedl verified the insulator activity at the scs region—one Drosophila hsp70 gene DNasel hypersensitive site in 1992. Zhao found and purified the scs binding protein BEAF, which bind and interact with scs in 1995. Studying the gene regulation in the chromatin level could find the genuine gene regulation mechanism in vivo. The method of analyzing the DNasel hypersensitive site was originally...