Cross‐linking of SsoII restriction endonuclease to cognate and non‐cognate DNAs

FEBS Letters

Nikolskaya, I.I.¹  Gromova, E.S.²  Kubareva, E.A.²  Kuznetsova, S.A.²  Shabarova, Z.A.²  Karyagina, A.S.¹  Sheflyan, G.Ya.² 

[1] Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Pogodinskaya str. 10, Moscow 119121, Russian Federation;A.N. Belozersky Institute of Physical and Chemical Biology and Chemistry Department, Moscow State University, Moscow 119899, Russian Federation

关键词: DNA-protein interaction;    Restriction endonuclease;    Duplex with active internucleotide group;    Covalent attachment;    MeIm;    N-methylimidazole;    DTT;    Dithiothreitol;   

DOI  :  10.1016/0014-5793(96)00645-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Specific and non-specific interactions SsoII restriction endonuclease (R·SsoII) were probed by the method of covalent attachment to modified DNA containing an active monosubstituted pyrophosphate internucleotide bond instead of a phosphodiester one. R·SsoII with six N-terminal His residues was shown to be cross-linked to duplexes with this type of modification, either containing or not the recognition sequence. Competition experiments with covalent attachment of R·SsoII to activated DNAs demonstrated the similar affinity of the enzyme to cognate and non-cognate DNAs in the absence of cofactor, Mg²⁺ ions.

【 授权许可】

Unknown