Creating a Ribonuclease T-tat That Preferentially Recognizes and Hydrolyzes HIV-1 TAR RNA in Vitro and in Vivo

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 2007 Dec 19

PMID 18086702

Citations 3

Authors

Chen Dow-Tien

Tsai Yuan-Jhih

Lin Alan

Affiliations

Soon will be listed here.

Abstract

A ribonuclease, RNase T-tat, specifically designed to hydrolyze the TAR RNA of HIV-1 virus has been engineered. The protein was made by domain swapping the TAT peptide at the loop 3 position of ribonuclease T1. The RNase T-tat maintains a guanine-specific RNA hydrolytic activity, and characteristically displayed a specific affinity for the TAR RNA of HIV-1. In the in vitro and in vivo assays, the RNase T-tat preferentially inhibited the expression of TAR-bearing mRNA through cis-TAR targeting, suggesting that RNase T-tat may be potentially useful for the disruption of the initial stage of the transcription process of HIV-1 virus.

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