title: Targeting DNA double-strand breaks with TAL effector nucleases.
abstract: Engineered nucleases that cleave specific DNA sequences in vivo are valuable reagents for targeted mutagenesis. Here we report a new class of sequence-specific nucleases created by fusing transcription activator-like effectors (TALEs) to the catalytic domain of the FokI endonuclease. Both native and custom TALE-nuclease fusions direct DNA double-strand breaks to specific, targeted sites.
authors.affiliation: Department of Plant Pathology, Iowa State University, Ames, Iowa 50011, USA.
authors.forename: Michelle
authors.initials: M
authors.lastname: Christian
authors.forename: Tomas
authors.initials: T
authors.lastname: Cermak
authors.forename: Erin L
authors.initials: EL
authors.lastname: Doyle
authors.forename: Clarice
authors.initials: C
authors.lastname: Schmidt
authors.forename: Feng
authors.initials: F
authors.lastname: Zhang
authors.forename: Aaron
authors.initials: A
authors.lastname: Hummel
authors.forename: Adam J
authors.initials: AJ
authors.lastname: Bogdanove
authors.forename: Daniel F
authors.initials: DF
authors.lastname: Voytas
mesh_terms: D001665:Binding Sites / Q000235:genetics; D020134:Catalytic Domain / Q000235:genetics; D004247:DNA / Q000235:genetics; D053903:DNA Breaks, Double-Stranded; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D015252:Deoxyribonucleases, Type II Site-Specific / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D018390:Gene Targeting; D005818:Genetic Engineering; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic; D015533:Transcriptional Activation; D014974:Xanthomonas; D016959:Xanthomonas campestris; D016335:Zinc Fingers / Q000235:genetics
chemical_list: D004268:DNA-Binding Proteins; D011993:Recombinant Fusion Proteins; D014157:Transcription Factors; D004247:DNA; C035042:endodeoxyribonuclease FokI; D015252:Deoxyribonucleases, Type II Site-Specific