| Literature DB >> 23189557 |
S A Sekerina, A V Grishin, A Iu Riazanova, R I Artiukh, E A Rogulin, A K Iunusova, T S Oretskaia, L A Zheleznaia, E A Kubareva.
Abstract
Ability of site-specific nickase BspD6I (Nt.BspD6I) to oligomerize at concentrations > or = 0.5 microM (> or = 0.035 mg/mL) is studied. Three states of Nt.BspD6I are registered via electrophoretic studies both in the presence and in the absence of DNA. Estimation of their molecular mass allows assigning them as a monomer, a dimer and a trimer. Both dimeric and monomeric Nt.BspD6I are shown to hydrolyze its DNA substrate with the identical specificity. Calculation of the electrostatic potential distribution on the Nt.BspD6I globule surface shows that the protein molecule is a dipole. The Nt. BspD6I oligomeric forms are likely to be the result of ionic protein interactions.Mesh：
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Year: 2012 PMID： 23189557 DOI： 10.1134/s1068162012040127
Source DB: PubMed Journal: Bioorg Khim ISSN： 0132-3423