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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...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2008
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Materias: | |
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. |
format | Text |
id | pubmed-2241915 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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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