Hybrid restriction enzymes: Zinc finger fusions to Fok I cleavage domain

被引：1420

作者：

Kim, YG ^{[1
]}

Cha, J ^{[1
]}

Chandrasegaran, S ^{[1
]}

机构：

[1] JOHNS HOPKINS UNIV, SCH HYG & PUBL HLTH, DEPT ENVIRONM HLTH SCI, BALTIMORE, MD 21205 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1996年 / 93卷 / 03期

关键词：

Flavobacterium okeanokoites; chimeric restriction endonuclease; protein engineering; recognition and cleavage domains;

D O I：

10.1073/pnas.93.3.1156

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：1156 / 1160

页数：5

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