Expression of Histone-based Fusion Protein HNHG in E.coli

DAI Fei-Han, CHEN Yan, GONG Yi, YANG Sheng-Li, TIAN Pei-Kun, Gu Jian-Ren*

(State Key Laboratory of Oncogenes and Related Genes, Shanghai Cancer Institute , Shanghai 200032, China; 1Shanghai Research Center of Biotechnology, the Chinese Academy of Sciences, Shanghai 200233, China )

Abstract

Histone H1 contributes to condense nucleosome into super-structure during the transformation of chromatin into chromosome. It is shown in this report that the fusion protein HNHG with the core of C-terminus of histone H10 expressed in BL21 (DE3) could also condense the plasmid DNA, just as histones did in nucleus. Under electron microscope, plasmid DNA condensed and supercoiled after t he addition of HNHG, in contrast to plasmid DNA control. This specific ability of the fusion protein HNHG of binding and condensing plasmids could be utilized to construct novel exogenous gene delivery systems. HNHG would be a promising can didate for gene delivery.

Key words engineered protein; histone H10; gene delivery system

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