INTERACTION OF THE MBOII RESTRICTION-ENDONUCLEASE WITH DNA

被引：11

作者：

SEKTAS, M ^{[1
]}

KACZOROWSKI, T ^{[1
]}

PODHAJSKA, AJ ^{[1
]}

机构：

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

来源：

GENE | 1995年 / 157卷 / 1-2期

关键词：

DNASE I FOOTPRINTING; EQUILIBRIUM BINDING CONSTANT; GEL MOBILITY SHIFT ASSAY; MORAXELLA BOVIS; PROTEIN-DNA INTERACTION;

D O I：

10.1016/0378-1119(94)00742-B

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

The binding of the MboII restriction endonuclease (R . MboII; ENase) to DNA containing its recognition site was investigated using a mobility shift assay. R . MboII forms specific, stable and immunodetectable complexes with its canonical target sequence. The association constant (K-a) of R . MboII was calculated to be 2.8 x 10(9)/M, and is about 10(4)-fold higher than the K-a value for non-specific binding. Based on results obtained after sedimentation of the R . MboII-DNA complex in a glycerol gradient and measurement of the retardation of the complexes in polyacrylamide gels, we conclude that specific binding to the canonical sequence involves a monomer of R . MboII. DNase I footprinting has shown that the enzyme covers 16 nucleotides of DNA on the 5'-GAAGA-3' strand.

引用

页码：181 / 185

页数：5

共 23 条

[11] PROPERTIES AND SUBUNIT STRUCTURE OF ECORV METHYLTRANSFERASE [J].