Class-IIS restriction enzymes — a review
Copyright policy )Class-IIS restriction enzymes — a review
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.
- University of Gdańsk Poland
- Korea Advanced Institute of Science and Technology Korea (Republic of)
- University of Wisconsin Hospital and Clinics United States
- University of Wisconsin–Madison United States
- UW Carbone Cancer Center United States
Base Sequence, Molecular Sequence Data, Restriction Mapping, Nucleic Acid Conformation, DNA, Deoxyribonucleases, Type II Site-Specific, Substrate Specificity
Base Sequence, Molecular Sequence Data, Restriction Mapping, Nucleic Acid Conformation, DNA, Deoxyribonucleases, Type II Site-Specific, Substrate Specificity
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