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Binding of two zinc finger nuclease monomers to two specific sites is required for effective double-strand DNA cleavage.

Abstract：

:Custom-designed zinc finger nucleases (ZFNs) are becoming powerful tools in gene targeting-the process of replacing a gene within a genome by homologous recombination. Here, we have studied the DNA cleavage by one such ZFN, DeltaQNK-FN, in order to gain insight into how ZFNs cleave DNA and how two inverted sites promote double-strand cleavage. DNA cleavage by DeltaQNK-FN is greatly facilitated when two DeltaQNK-binding sites are close together in an inverted orientation. Substrate cleavage was not first order with respect to the concentration of DeltaQNK-FN, indicating that double-strand cleavage requires dimerization of the FokI cleavage domain. Rates of DNA cleavage decrease as the substrate concentrations increase, suggesting that the DeltaQNK-FN molecules are effectively "trapped" in a 1:1 complex on DNA when the DNA is in excess. The physical association of two ZFN monomers on DNA was monitored by using the biotin-pull-down assay, which showed that the formation of DeltaQNK-FN active complex required both binding of the two DeltaQNK-FN molecules to specific DNA sites and divalent metal ions.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Mani M,Smith J,Kandavelou K,Berg JM,Chandrasegaran S

doi

10.1016/j.bbrc.2005.07.021

subject

Has Abstract

pub_date

2005-09-09 00:00:00

pages

1191-1197

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)01485-3

journal_volume

334

pub_type

杂志文章

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