Oligomerization of site-specific nicking endonuclease BspD6I at high protein concentrations

The ability of site-specific nicking endonuclease BspD6I (Nt.BspD6I) to oligomerize at concentrations > 0.5 μM (>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 allo...

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Bibliographic Details
Published in:Russian journal of bioorganic chemistry 2012-07, Vol.38 (4), p.376-382
Main Authors: Sekerina, S. A., Grishin, A. V., Ryazanova, A. Yu, Artyukh, R. I., Rogulin, E. A., Yunusova, A. K., Oretskaya, T. S., Zheleznaya, L. A., Kubareva, E. A.
Format: Article
Language:English
Subjects:
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
DNA
Electrostatic properties
Endonuclease
Life Sciences
Monomers
Nicking
Oligomerization
Organic Chemistry
Protein interaction
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Summary:The ability of site-specific nicking endonuclease BspD6I (Nt.BspD6I) to oligomerize at concentrations > 0.5 μM (>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 same 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-protein interactions.
ISSN:1068-1620
1608-330X
DOI:10.1134/S1068162012040127