| Literature DB >> 11944931 |
Xiang-duo Kong1, Shi-zhen Zhu, Xiao-jun Gou, Xiao-ping Wang, Hong-ying Zhang, Jin Zhang.
Abstract
A circular RNA-DNA enzyme with higher activity to target RNA cleavage and higher stability than that of the hammerhead ribozyme in the presence of RNase A was obtained by in vitro selection. The molecule is composed of a catalytic domain of 22-mer ribonucleotides derived from the hammerhead ribozyme and a fragment of 55-mer deoxyribonucleotides. The DNA fragment contains two substrate-binding domains (9-mer and 6-mer, respectively) and a "regulation domain" (assistant 40-mer DNA with 20-mer random deoxyribonucleotides sequence), which probably play the role in the regulation of flexibility and rigidity of the circular RNA-DNA enzyme. The above results suggest that the circular RNA-DNA enzyme will have a great prospect in gene-targeting therapies. (c)2002 Elsevier Science (USA).Entities:
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Year: 2002 PMID: 11944931 DOI: 10.1006/bbrc.2002.6767
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575