Document Detail

Expression of histone-based fusion protein HNHG in E.coli
MedLine Citation:
PMID:  12417928     Owner:  NLM     Status:  MEDLINE    
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.
Fei-Han Dai; Yan Chen; Yi Gong; Sheng-Li Yang; Pei-Kun Tian; Jian-Ren Gu
Publication Detail:
Type:  English Abstract; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica     Volume:  34     ISSN:  0582-9879     ISO Abbreviation:  Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao     Publication Date:  2002 Nov 
Date Detail:
Created Date:  2002-11-05     Completed Date:  2003-03-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  20730160R     Medline TA:  Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai)     Country:  China    
Other Details:
Languages:  chi     Pagination:  800-3     Citation Subset:  IM    
State Key Laboratory of Oncogenes and Related Genes, Shanghai Cancer Institute, Shanghai 200032, China.
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MeSH Terms
DNA, Superhelical / genetics,  metabolism,  ultrastructure
Electrophoretic Mobility Shift Assay
Gene Expression
Histones / genetics*,  metabolism
Microscopy, Electron
Plasmids / genetics,  metabolism,  ultrastructure
Protein Binding
Recombinant Fusion Proteins / genetics,  metabolism
Reg. No./Substance:
0/DNA, Superhelical; 0/Histones; 0/Recombinant Fusion Proteins

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