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TAL nucleases (TALNs): hybrid proteins composed of TAL effectors and FokI DNA-cleavage domain
DNA double-strand breaks enhance homologous recombination in cells and have been exploited for targeted genome editing through use of engineered endonucleases. Here we report the creation and initial characterization of a group of rare-cutting, site-specific DNA nucleases produced by fusion of the r...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3017587/ https://www.ncbi.nlm.nih.gov/pubmed/20699274 http://dx.doi.org/10.1093/nar/gkq704 |
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author | Li, Ting Huang, Sheng Jiang, Wen Zhi Wright, David Spalding, Martin H. Weeks, Donald P. Yang, Bing |
author_facet | Li, Ting Huang, Sheng Jiang, Wen Zhi Wright, David Spalding, Martin H. Weeks, Donald P. Yang, Bing |
author_sort | Li, Ting |
collection | PubMed |
description | DNA double-strand breaks enhance homologous recombination in cells and have been exploited for targeted genome editing through use of engineered endonucleases. Here we report the creation and initial characterization of a group of rare-cutting, site-specific DNA nucleases produced by fusion of the restriction enzyme FokI endonuclease domain (FN) with the high-specificity DNA-binding domains of AvrXa7 and PthXo1. AvrXa7 and PthXo1 are members of the transcription activator-like (TAL) effector family whose central repeat units dictate target DNA recognition and can be modularly constructed to create novel DNA specificity. The hybrid FN-AvrXa7, AvrXa7-FN and PthXo1-FN proteins retain both recognition specificity for their target DNA (a 26 bp sequence for AvrXa7 and 24 bp for PthXo1) and the double-stranded DNA cleaving activity of FokI and, thus, are called TAL nucleases (TALNs). With all three TALNs, DNA is cleaved adjacent to the TAL-binding site under optimal conditions in vitro. When expressed in yeast, the TALNs promote DNA homologous recombination of a LacZ gene containing paired AvrXa7 or asymmetric AvrXa7/PthXo1 target sequences. Our results demonstrate the feasibility of creating a tool box of novel TALNs with potential for targeted genome modification in organisms lacking facile mechanisms for targeted gene knockout and homologous recombination. |
format | Text |
id | pubmed-3017587 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-30175872011-01-10 TAL nucleases (TALNs): hybrid proteins composed of TAL effectors and FokI DNA-cleavage domain Li, Ting Huang, Sheng Jiang, Wen Zhi Wright, David Spalding, Martin H. Weeks, Donald P. Yang, Bing Nucleic Acids Res Synthetic Biology and Chemistry DNA double-strand breaks enhance homologous recombination in cells and have been exploited for targeted genome editing through use of engineered endonucleases. Here we report the creation and initial characterization of a group of rare-cutting, site-specific DNA nucleases produced by fusion of the restriction enzyme FokI endonuclease domain (FN) with the high-specificity DNA-binding domains of AvrXa7 and PthXo1. AvrXa7 and PthXo1 are members of the transcription activator-like (TAL) effector family whose central repeat units dictate target DNA recognition and can be modularly constructed to create novel DNA specificity. The hybrid FN-AvrXa7, AvrXa7-FN and PthXo1-FN proteins retain both recognition specificity for their target DNA (a 26 bp sequence for AvrXa7 and 24 bp for PthXo1) and the double-stranded DNA cleaving activity of FokI and, thus, are called TAL nucleases (TALNs). With all three TALNs, DNA is cleaved adjacent to the TAL-binding site under optimal conditions in vitro. When expressed in yeast, the TALNs promote DNA homologous recombination of a LacZ gene containing paired AvrXa7 or asymmetric AvrXa7/PthXo1 target sequences. Our results demonstrate the feasibility of creating a tool box of novel TALNs with potential for targeted genome modification in organisms lacking facile mechanisms for targeted gene knockout and homologous recombination. Oxford University Press 2011-01 2010-08-10 /pmc/articles/PMC3017587/ /pubmed/20699274 http://dx.doi.org/10.1093/nar/gkq704 Text en © The Author(s) 2010. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Synthetic Biology and Chemistry Li, Ting Huang, Sheng Jiang, Wen Zhi Wright, David Spalding, Martin H. Weeks, Donald P. Yang, Bing TAL nucleases (TALNs): hybrid proteins composed of TAL effectors and FokI DNA-cleavage domain |
title | TAL nucleases (TALNs): hybrid proteins composed of TAL effectors and FokI DNA-cleavage domain |
title_full | TAL nucleases (TALNs): hybrid proteins composed of TAL effectors and FokI DNA-cleavage domain |
title_fullStr | TAL nucleases (TALNs): hybrid proteins composed of TAL effectors and FokI DNA-cleavage domain |
title_full_unstemmed | TAL nucleases (TALNs): hybrid proteins composed of TAL effectors and FokI DNA-cleavage domain |
title_short | TAL nucleases (TALNs): hybrid proteins composed of TAL effectors and FokI DNA-cleavage domain |
title_sort | tal nucleases (talns): hybrid proteins composed of tal effectors and foki dna-cleavage domain |
topic | Synthetic Biology and Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3017587/ https://www.ncbi.nlm.nih.gov/pubmed/20699274 http://dx.doi.org/10.1093/nar/gkq704 |
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