Structure subtraction as an approach to investigation of the mechanism of restriction enzyme action

FEBS Letters

Gorbunov, J.A.¹  Baclanov, M.M.¹  Malygin, E.G.¹  Popov, S.G.¹  Zinoviev, V.V.¹ 

[1] All-Union Scientific Research Institute of Molecular Biology, Koltsovo, Novosibirsk Region, 633159, USSR

关键词: Restriction endonuclease;    Oligonucleotides;    Specificity;    Recognition site;   

DOI  :  10.1016/0014-5793(83)80166-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Endonuclease BamHI 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. BamHI was found not to hydrolyse the phosphodiester bonds outside the double helix. Also BamHI forms a productive complex with the non-symmetrical substrate, having half the recognition sites, of a single strand.

【 授权许可】

Unknown