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Gene. 1991 Apr;100:13-26.

Class-IIS restriction enzymes--a review.

Author information

1
McArdle Laboratory for Cancer Research, University of Wisconsin, Madison 53706.

Erratum in

  • Gene 1991 Dec 20;109(1):169.

Abstract

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.

PMID:
2055464
DOI:
10.1016/0378-1119(91)90345-c
[Indexed for MEDLINE]

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