CLASS-IIS RESTRICTION ENZYMES - A REVIEW

被引：203

作者：

SZYBALSKI, W ^{[1
]}

KIM, SC ^{[1
]}

HASAN, N ^{[1
]}

PODHAJSKA, AJ ^{[1
]}

机构：

[1] UNIV GDANSK, DEPT MICROBIOL, PL-80822 GDANSK, POLAND

来源：

GENE | 1991年 / 100卷

关键词：

RECOMBINANT DNA; ENDONUCLEASES; METHYLTRANSFERASES; PROBES; RECOGNITION AND CLEAVAGE DOMAINS; TRIMMING VECTORS;

D O I：

10.1016/0378-1119(91)90345-C

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

Class-IIS restriction enzymes (ENases-IIS) interact with two discrete sites on double-stranded DNA: the recognition site, which is 4-7 bp long, and the cleavage site, usually 1-20 bp away from the recognition site. The recognition sequences of ENases-IIS are totally (or partially) asymmetric and all of the characterized ENases-IIS are monomeric. A total of 35 ENases-IIS are described (80, if all isoschizomers are taken into consideration) together with ten related ENases (class IIT), and 15 cognate methyltransferases (MTases-IIS). The physical, chemical, and molecular properties of the ENases-IIS and MTases-IIS are reviewed and many unique applications of this class of enzymes are described, including: precise trimming of DNA; retrieval of cloned fragments; gene assembly; use as a universal restriction enzyme; cleavage of single-stranded DNA; detection of point mutations; tandem amplification; printing-amplification reaction; and localization of methylated bases.

引用

页码：13 / 26

页数：14

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