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Int. J. Mol. Sci. 2013, 14(12), 23842-23857; doi:10.3390/ijms141223842
Article

A Histone-Like Protein Induces Plasmid DNA to Form Liquid Crystals in Vitro and Gene Compaction in Vivo

1,2,* , 1
,
1,* , 2
 and
2
1 Key Laboratory of Solid Waste Treatment and Resource Recycle & Fundamental Science on Nuclear Waste and Environmental Security Laboratory, Southwest University of Science and Technology, Mianyang 621010, Sichuan, China 2 School of Environment and Resource, Southwest University of Science and Technology, Mianyang 621010, Sichuan, China
* Authors to whom correspondence should be addressed.
Received: 30 October 2013 / Revised: 17 November 2013 / Accepted: 21 November 2013 / Published: 6 December 2013
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Abstract

The liquid crystalline state is a universal phenomenon involving the formation of an ordered structure via a self-assembly process that has attracted attention from numerous scientists. In this study, the dinoflagellate histone-like protein HCcp3 is shown to induce super-coiled pUC18 plasmid DNA to enter a liquid crystalline state in vitro, and the role of HCcp3 in gene condensation in vivo is also presented. The plasmid DNA (pDNA)-HCcp3 complex formed birefringent spherical particles with a semi-crystalline selected area electronic diffraction (SAED) pattern. Circular dichroism (CD) titrations of pDNA and HCcp3 were performed. Without HCcp3, pUC18 showed the characteristic B conformation. As the HCcp3 concentration increased, the 273 nm band sharply shifted to 282 nm. When the HCcp3 concentration became high, the base pair (bp)/dimer ratio fell below 42/1, and the CD spectra of the pDNA-HCcp3 complexes became similar to that of dehydrated A-form DNA. Microscopy results showed that HCcp3 compacted the super-coiled gene into a condensed state and that inclusion bodies were formed. Our results indicated that HCcp3 has significant roles in gene condensation both in vitro and in histone-less eukaryotes in vivo. The present study indicates that HCcp3 has great potential for applications in non-viral gene delivery systems, where HCcp3 may compact genetic material to form liquid crystals.
Keywords: liquid crystal; gene condensation; plasmid; histone-like protein; non-viral gene delivery liquid crystal; gene condensation; plasmid; histone-like protein; non-viral gene delivery
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
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Sun, S.; Liu, M.; Dong, F.; Fan, S.; Yao, Y. A Histone-Like Protein Induces Plasmid DNA to Form Liquid Crystals in Vitro and Gene Compaction in Vivo. Int. J. Mol. Sci. 2013, 14, 23842-23857.

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