Engineering novel restriction endonucleases: Principles and applications

被引:39
作者
Jeltsch, A
Wenz, C
Wende, W
Selent, U
Pingoud, A
机构
关键词
D O I
10.1016/0167-7799(96)10030-5
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Restriction endonucleases cleave DNA with remarkable sequence specificity. In this review, we summarize the status of, and prospects for, engineering restriction endonucleases with new specificities. Such variants could be of considerable commercial value because restriction enzymes are among the most frequently used enzymes in molecular biology, and not all the desirable specificities are available. While it has not yet been possible to effect specificity changes, mutants have been described that (1) exhibit relaxed specificity, (2) favour modified substrates over their natural substrates, (3) discriminate between cleavage sites located in different sequences, (4) prefer metal ions other than Mg2+ as cofactors for cleavage, or (5) possess site-specific DNA-nicking activity.
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页码:235 / 238
页数:4
相关论文
共 34 条
[1]   CHANGING THE HYDROGEN-BONDING POTENTIAL IN THE DNA-BINDING SITE OF ECORI BY SITE-DIRECTED MUTAGENESIS DRASTICALLY REDUCES THE ENZYMATIC-ACTIVITY, NOT, HOWEVER, THE PREFERENCE OF THIS RESTRICTION ENDONUCLEASE FOR CLEAVAGE WITHIN THE SITE -GAATTC- [J].
ALVES, J ;
RUTER, T ;
GEIGER, R ;
FLIESS, A ;
MAASS, G ;
PINGOUD, A .
BIOCHEMISTRY, 1989, 28 (06) :2678-2684
[2]   ACCURACY OF THE ECORV RESTRICTION-ENDONUCLEASE - BINDING AND CLEAVAGE STUDIES WITH OLIGODEOXYNUCLEOTIDE SUBSTRATES CONTAINING DEGENERATE RECOGNITION SEQUENCES [J].
ALVES, J ;
SELENT, U ;
WOLFES, H .
BIOCHEMISTRY, 1995, 34 (35) :11191-11197
[3]  
Bickle TA, 1993, NUCLEASES, P89
[4]   STRUCTURE OF PVUII ENDONUCLEASE WITH COGNATE DNA [J].
CHENG, XD ;
BALENDIRAN, K ;
SCHILDKRAUT, I ;
ANDERSON, JE .
EMBO JOURNAL, 1994, 13 (17) :3927-3935
[5]   SATURATION MUTAGENESIS OF HIS(114) OF ECORI REVEALS RELAXED-SPECIFICITY MUTANTS [J].
FLORES, H ;
OSUNA, J ;
HEITMAN, J ;
SOBERON, X .
GENE, 1995, 157 (1-2) :295-301
[6]   GENETIC-ENGINEERING OF ECORI MUTANTS WITH ALTERED AMINO-ACID RESIDUES IN THE DNA-BINDING SITE - PHYSICOCHEMICAL INVESTIGATIONS GIVE EVIDENCE FOR AN ALTERED MONOMER DIMER EQUILIBRIUM FOR THE GLN144LYS145 AND GLN144LYS145LYS200 MUTANTS [J].
GEIGER, R ;
RUTER, T ;
ALVES, J ;
FLIESS, A ;
WOLFES, H ;
PINGOUD, V ;
URBANKE, C ;
MAASS, G ;
PINGOUD, A ;
DUSTERHOFT, A ;
KROGER, M .
BIOCHEMISTRY, 1989, 28 (06) :2667-2677
[7]  
HAGER PW, 1990, J BIOL CHEM, V265, P21520
[8]   MODES OF DNA CLEAVAGE BY THE ECORV RESTRICTION ENDONUCLEASE [J].
HALFORD, SE ;
GOODALL, AJ .
BIOCHEMISTRY, 1988, 27 (05) :1771-1777
[9]  
Heitman J, 1993, Genet Eng (N Y), V15, P57
[10]   MUTANTS OF THE ECORI ENDONUCLEASE WITH PROMISCUOUS SUBSTRATE-SPECIFICITY IMPLICATE RESIDUES INVOLVED IN SUBSTRATE RECOGNITION [J].
HEITMAN, J ;
MODEL, P .
EMBO JOURNAL, 1990, 9 (10) :3369-3378