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Structure subtraction as an approach to investigation of the mechanism of restriction enzyme action
Author(s) -
Zinoviev V.V.,
Gorbunov J.A.,
Baclanov M.M.,
Popov S.G.,
Malygin E.G.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80166-5
Subject(s) - phosphodiester bond , endonuclease , oligonucleotide , dna , cleavage (geology) , guanine , stereochemistry , duplex (building) , nucleotide , chemistry , restriction enzyme , recognition sequence , biochemistry , active site , enzyme , biology , rna , gene , paleontology , fracture (geology)
Endonuclease Bam HI cleaves the phosphodiester bonds between the guanine residues within the duplex DNA sequence G↓GATCC. The substrate characteristics of oligonucleotides, containing some defects in the sequence recognized by endonuclease (nick, absence of some internucleotide phosphate or nucleotide, partially single‐stranded form of the recognition site) were investigated. The results suggest that the specificity of synthetic oligonucleotide cleavage is strongly dependent on the ribosophosphate backbone intactness inside the recognition site. Bam HI was found not to hydrolyse the phosphodiester bonds outside the double helix. Also Bam HI forms a productive complex with the non‐symmetrical substrate, having half the recognition sites, of a single strand.