Earticle

초록

영어

Protein-based gene delivery including histone proteins has recently emerged as a powerful technique for non-viral DNA transfer. Histones are DNA-binding proteins that function in DNA packaging and protection. Several studies have examined the use of full-length histone H1-mediated gene transfer, and a few studies have investigated the use of C-terminal histone H1 fragments as gene-transfer materials. Previously, we cloned a novel histone H1 cDNA from the goldfish Carassius auratus and found that a recombinant histone H1 C-terminal short peptide (H1C) of 61 amino acids has comparable DNA binding and protection functions as full-length histone H1. In the present work, we successfully expressed and purified soluble recombinant H1C in an Escherichia coli expression system using a hexahistidine tag fusion strategy and providing tRNAs for rare codons. We confirmed its DNA-binding ability and found that this H1C peptide had similar or higher transfection efficiency in mammalian cells than the widely used agent lipofectamine. Therefore, we suggest that this novel goldfish-derived recombinant histone H1 C-terminal short peptide could be used as a peptide-based gene-transfer mediator.

키워드

저자

• Dong Soo Hwang [ Department of Chemical Engineering, bInstitute of Environmental and Energy Technology, POSTECH, Equal contribution ]
• Hee Jung Jung [ Department of Chemical Engineering, Equal contribution ]
• Quan De Wei [ Department of Chemical Engineering, Center for Disease Control and Prevention of Zhuhai ]
• Hyung Joon Cha [ Department of Chemical Engineering ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576