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

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• 作者：S. A. Sekerina (1)
  A. V. Grishin (1)
  A. Yu. Ryazanova (1)
  R. I. Artyukh (2)
  E. A. Rogulin (2)
  A. K. Yunusova (2)
  T. S. Oretskaya (1)
  L. A. Zheleznaya (2)
  E. A. Kubareva (1) kubareva@belozersky.msu.ru
• 关键词：heterodimeric restriction endonucleases – ; nicking endonuclease – ; oligomerization – ; protein docking
• 刊名：Russian Journal of Bioorganic Chemistry
• 出版年：2012
• 出版时间：July 2012
• 年：2012
• 卷：38
• 期：4
• 页码：376-382
• 全文大小：498.4 KB
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• 作者单位：1. Chemistry Department, Faculty of Bioengineering and Bioinformatics and A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119991 Leninskie Gory 1, Moscow, Russia2. Institute of Theoretical and Experimental Biophysics, ul. Institutskaya 3, Pushchino, 142290 Russia
• ISSN：1608-330X

文摘

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.