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Synthetic protein-protein interaction domains created by shuffling Cys2His2 zinc-fingers.

Authors :
Giesecke AV
Fang R
Joung JK
Source :
Molecular systems biology [Mol Syst Biol] 2006; Vol. 2, pp. 2006.2011. Date of Electronic Publication: 2006 Mar 21.
Publication Year :
2006

Abstract

Cys2His2 zinc-fingers (C2H2 ZFs) mediate a wide variety of protein-DNA and protein-protein interactions. DNA-binding C2H2 ZFs can be shuffled to yield artificial proteins with different DNA binding specificities. Here we demonstrate that shuffling of C2H2 ZFs from transcription factor dimerization zinc-finger (DZF) domains can also yield two-finger DZFs with novel protein-protein interaction specificities. We show that these synthetic protein-protein interaction domains can be used to mediate activation of a single-copy reporter gene in bacterial cells and of an endogenous gene in human cells. In addition, the synthetic two-finger domains we constructed can also be linked together to create more extended, four-finger interfaces. Our results demonstrate that shuffling of C2H2 ZFs can yield artificial protein-interaction components that should be useful for applications in synthetic biology.

Details

Language :
English
ISSN :
1744-4292
Volume :
2
Database :
MEDLINE
Journal :
Molecular systems biology
Publication Type :
Academic Journal
Accession number :
16732192
Full Text :
https://doi.org/10.1038/msb4100053