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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...

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Autores principales: Li, Ting, Huang, Sheng, Jiang, Wen Zhi, Wright, David, Spalding, Martin H., Weeks, Donald P., Yang, Bing
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2011
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.
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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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