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632943 comments
ZFPs are typically first tested for activity in vitro using ELISA assays and then using a yeast expression system.
In other embodiments, ZFPs with nuclease activity are designed.
In other embodiments, the nuclease domain(s) are nickases in that they induce single-stranded break.
Such nickases are described for example in U.S. Non-limiting examples of such linkers are described, for example, in U.S.
Optimal levels of cleavage can also depend on both the distance
between the binding sites of the two fusion proteins (see,
for example, Smith et al. In addition, the structure of the fusion proteins
and the distance between the target sites can influence whether cleavage
occurs adjacent a single nucleotide pair, or whether cleavage occurs at several
sites. In cases where two fusion proteins, each comprising a cleavage half-domain, are used,
the distance between the near edges of the binding sites can be 1, 2, 3, 4, 5, 6,
7, 8, 9, 10, 25 or more nucleotides (or any integral value between 1 and
50 nucleotides). Accordingly, the methods described herein contemplate the use of
a dominant-negative mutant of a nuclease (or a nucleic acid encoding same) that is
expressed in a cell along with the two fusion proteins.
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