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. 2012 Aug;16(3-4):268-77.
doi: 10.1016/j.cbpa.2012.06.007. Epub 2012 Jul 20.

Advances in Targeted Genome Editing

Free PMC article

Advances in Targeted Genome Editing

Pablo Perez-Pinera et al. Curr Opin Chem Biol. .
Free PMC article


New technologies have recently emerged that enable targeted editing of genomes in diverse systems. This includes precise manipulation of gene sequences in their natural chromosomal context and addition of transgenes to specific genomic loci. This progress has been facilitated by advances in engineering targeted nucleases with programmable, site-specific DNA-binding domains, including zinc finger proteins and transcription activator-like effectors (TALEs). Recent improvements have enhanced nuclease performance, accelerated nuclease assembly, and lowered the cost of genome editing. These advances are driving new approaches to many areas of biotechnology, including biopharmaceutical production, agriculture, creation of transgenic organisms and cell lines, and studies of genome structure, regulation, and function. Genome editing is also being investigated in preclinical and clinical gene therapies for many diseases.


Figure 1
Figure 1. Milestones in genome editing and accelerated progress in nuclease engineering
An estimate of the number of articles referring to genome editing is shown for each year with specific reference to major advances. Data for this graph was obtained from the Web of ScienceSM by searching for articles referencing “zinc finger nuclease OR tale nuclease”.
Figure 2
Figure 2. Three dimensional structure of a Zinc Finger Protein and TAL effector
(A) Front and lateral view of a six-finger zinc finger protein that consists of six tandem repeats of C2H2 zinc finger motifs, each consisting of approximately 30 amino acids. A single zinc finger, which recognizes 3 bp of DNA, consists of an α helix and two antiparallel β sheets that coordinate with a zinc ion through two histidine residues and two cysteine residues. Contacts with DNA are made through interactions with side chains on the α helix. (B) TAL effectors consist of repeats of 34 amino acids that recognize one single bp of DNA. Each of these units is formed by two nearly identical alpha helices flanking two variant amino acids, known as the repeat variable di-residue, that determine the binding specificity. The structures have been modeled using MacPyMOL with Protein Data Bank files 1P47 (crystal structure of tandem Zif268 molecules complexed to DNA) and 3UGM (structure of TAL effector PthXo1 bound to its DNA target).

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