Expression of histone-based fusion protein HNHG in E.coli

Histone H1 contributes to condense nucleosome into super-structure during the transformation of chromatin into chromosome. It is shown in this rep or t that the fusion protein HNHG with the core of C-terminus of histone H1(0) expressed in BL21 (DE3) could also condense the plasmid DNA, just as histo...

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Published inSheng wu hua hsüeh yü sheng wu wu li hsüeh pao Vol. 34; no. 6; p. 800
Main Authors Dai, Fei-Han, Chen, Yan, Gong, Yi, Yang, Sheng-Li, Tian, Pei-Kun, Gu, Jian-Ren
Format Journal Article
LanguageChinese
Published China 01.11.2002
Subjects
DNA, Superhelical - genetics
DNA, Superhelical - metabolism
DNA, Superhelical - ultrastructure
Electrophoretic Mobility Shift Assay
Gene Expression
Histones - genetics
Histones - metabolism
Humans
Microscopy, Electron
Plasmids - genetics
Plasmids - metabolism
Plasmids - ultrastructure
Protein Binding
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
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Summary:Histone H1 contributes to condense nucleosome into super-structure during the transformation of chromatin into chromosome. It is shown in this rep or t that the fusion protein HNHG with the core of C-terminus of histone H1(0) 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 candidate for gene delivery.
ISSN:0582-9879