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Hybrid restriction enzymes: zinc finger fusions to Fok I cleavage domain.

Kim, Y G, Cha, J, Chandrasegaran, S·1996·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.93.3.1156
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Abstract

A long-term goal in the field of restriction-modification enzymes has been to generate restriction endonucleases with novel sequence specificities by mutating or engineering existing enzymes. This will avoid the increasingly arduous task of extensive screening of bacteria and other microorganisms for new enzymes. Here, we report the deliberate creation of novel site-specific endonucleases by linking two different zinc finger proteins to the cleavage domain of Fok I endonuclease. Both fusion proteins are active and under optimal conditions cleave DNA in a sequence-specific manner. Thus, the modular structure of Fok I endonuclease and the zinc finger motifs makes it possible to create "artificial" nucleases that will cut DNA near a predetermined site. This opens the way to generate many new enzymes with tailor-made sequence specificities desirable for various applications.

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Research works printed but not linked: 23

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Metadata

Authors
Kim, Y. G., Cha, J., & Chandrasegaran, S.
Affiliations
Department of Environmental Health Sciences, Johns Hopkins University, School of Hygiene and Public Health, Baltimore, MD 21205-2179, USA.
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1996-02-06
Volume
93
Issue
3
Pages
1156-1160
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.93.3.1156
Cited by
1,889
References
2
Language
en

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