Breaking the code of DNA binding specificity of TAL-type III effectors

verfasst von: Jens Boch, Heidi Scholze, Sebastian Schornack, Angelika Landgraf, Simone Hahn, Sabine Kay, Thomas Lahaye, Anja Nickstadt, Ulla Bonas
Abstract: The pathogenicity of many bacteria depends on the injection of effector proteins via type III secretion into eukaryotic cells in order to manipulate cellular processes. TAL (transcription activator-like) effectors from plant pathogenic Xanthomonas are important virulence factors that act as transcriptional activators in the plant cell nucleus, where they directly bind to DNA via a central domain of tandem repeats. Here, we show how target DNA specificity of TAL effectors is encoded. Two hypervariable amino acid residues in each repeat recognize one base pair in the target DNA. Recognition sequences of TAL effectors were predicted and experimentally confirmed. The modular protein architecture enabled the construction of artificial effectors with new specificities. Our study describes the functionality of a distinct type of DNA binding domain and allows the design of DNA binding domains for biotechnology.
Externe Organisation(en): Martin-Luther-Universität Halle-Wittenberg
Typ: Artikel
Journal: Science
Band: 326
Seiten: 1509-1512
Anzahl der Seiten: 4
ISSN: 0036-8075
Publikationsdatum: 11.12.2009
Publikationsstatus: Veröffentlicht
Peer-reviewed: Ja
ASJC Scopus Sachgebiete: Allgemein
Elektronische Version(en): https://doi.org/10.1126/science.1178811 (Zugang: Geschlossen)

BibTeX

@article{8ecfef93a8dc4a15b3295a1975187026,
title = "Breaking the code of DNA binding specificity of TAL-type III effectors",
abstract = "The pathogenicity of many bacteria depends on the injection of effector proteins via type III secretion into eukaryotic cells in order to manipulate cellular processes. TAL (transcription activator-like) effectors from plant pathogenic Xanthomonas are important virulence factors that act as transcriptional activators in the plant cell nucleus, where they directly bind to DNA via a central domain of tandem repeats. Here, we show how target DNA specificity of TAL effectors is encoded. Two hypervariable amino acid residues in each repeat recognize one base pair in the target DNA. Recognition sequences of TAL effectors were predicted and experimentally confirmed. The modular protein architecture enabled the construction of artificial effectors with new specificities. Our study describes the functionality of a distinct type of DNA binding domain and allows the design of DNA binding domains for biotechnology.",
author = "Jens Boch and Heidi Scholze and Sebastian Schornack and Angelika Landgraf and Simone Hahn and Sabine Kay and Thomas Lahaye and Anja Nickstadt and Ulla Bonas",
note = "Copyright: Copyright 2010 Elsevier B.V., All rights reserved.",
year = "2009",
month = dec,
day = "11",
doi = "10.1126/science.1178811",
language = "English",
volume = "326",
pages = "1509--1512",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5959",
}