| Abstract: | Kinetic values of the BamHI endonuclease interaction with synthetic oligonucleotides, containing some defects, have been determined. These defects were: the absence of the one internucleotide phosphate in the GGATCC sequence; substitution of a phosphate linkage by a methylphosphonate one; 5'-protruding end of the double-stranded oligonucleotide substrate. Some modifications resulted in the increase of the initial rates of cleavage due to higher Vmax values for these substrates. Several structural defects in the oligonucleotide substrates have been shown to intensity the formation of productive complexes with the enzyme, which can be explained by the significant role of the polynucleotide chain kinks in the recognition process. Studies on oligonucleotides with different defects made it possible to reveal the phosphate groups essential for the interaction with BamHI endonuclease. |
