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Creating a ribonuclease T-tat that preferentially recognizes and hydrolyzes HIV-1 TAR RNA in vitro and in vivo

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 characteristica...

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Detalles Bibliográficos
Autores principales: Dow-Tien, Chen, Yuan-Jhih, Tsai, Alan, Lin
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2008
Materias:
RNA
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2241915/
https://www.ncbi.nlm.nih.gov/pubmed/18086702
http://dx.doi.org/10.1093/nar/gkm1118
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author Dow-Tien, Chen
Yuan-Jhih, Tsai
Alan, Lin
author_facet Dow-Tien, Chen
Yuan-Jhih, Tsai
Alan, Lin
author_sort Dow-Tien, Chen
collection PubMed
description 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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spelling pubmed-22419152008-02-21 Creating a ribonuclease T-tat that preferentially recognizes and hydrolyzes HIV-1 TAR RNA in vitro and in vivo Dow-Tien, Chen Yuan-Jhih, Tsai Alan, Lin Nucleic Acids Res RNA 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. Oxford University Press 2008-02 2007-12-17 /pmc/articles/PMC2241915/ /pubmed/18086702 http://dx.doi.org/10.1093/nar/gkm1118 Text en © 2007 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle RNA
Dow-Tien, Chen
Yuan-Jhih, Tsai
Alan, Lin
Creating a ribonuclease T-tat that preferentially recognizes and hydrolyzes HIV-1 TAR RNA in vitro and in vivo
title Creating a ribonuclease T-tat that preferentially recognizes and hydrolyzes HIV-1 TAR RNA in vitro and in vivo
title_full Creating a ribonuclease T-tat that preferentially recognizes and hydrolyzes HIV-1 TAR RNA in vitro and in vivo
title_fullStr Creating a ribonuclease T-tat that preferentially recognizes and hydrolyzes HIV-1 TAR RNA in vitro and in vivo
title_full_unstemmed Creating a ribonuclease T-tat that preferentially recognizes and hydrolyzes HIV-1 TAR RNA in vitro and in vivo
title_short Creating a ribonuclease T-tat that preferentially recognizes and hydrolyzes HIV-1 TAR RNA in vitro and in vivo
title_sort creating a ribonuclease t-tat that preferentially recognizes and hydrolyzes hiv-1 tar rna in vitro and in vivo
topic RNA
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2241915/
https://www.ncbi.nlm.nih.gov/pubmed/18086702
http://dx.doi.org/10.1093/nar/gkm1118
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