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A gene delivery system based on the N-terminal domain of human topoisomerase I

Paper ID Volume ID Publish Year Pages File Format Full-Text
7148 536 2011 11 PDF Available
Title
A gene delivery system based on the N-terminal domain of human topoisomerase I
Abstract

The N-terminal 200 amino acid residues of topoisomerase I (TopoN) is highly positive in charge and has DNA binding activity, without DNA sequence and topological specificity. Here, a fusion protein (6 × His-PTD-TopoN) containing a hexahistidine (6 × His) tag, a membrane penetration domain and TopoN (amino acid 3–200) was designed and developed. The protein can bind to different sizes (3.0–8.0 kb) and forms (circular and linear) of DNA and translocates the bound DNA to the nucleus. The protein also showed low cytotoxicity to GF-1 grouper fish fin cells that were previously very sensitive and difficult to transfect in vitro. Maintaining the hexahistidine tag increased the protein’s transfection efficiency in COS7 African green monkey kidney cells and simplified the purification process. The plasmid pEGFP-N1 was delivered into COS7 cells by the protein in ATP- and temperature-dependent manners. The results indicate that the binding ability of TopoN is very useful for DNA delivery and the carrier protein can be expressed in Escherichia coli without removal of the hexahistidine tag.

Keywords
Gene delivery system; Protein transduction domain; Topoisomerase I; Membrane penetration domain; DNA binding
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A gene delivery system based on the N-terminal domain of human topoisomerase I
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 32, Issue 17, June 2011, Pages 4174–4184
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us