Rapid purification of HU protein from Halobacillus karajensis
Journal: Molecular Biology Research Communications (Vol.3, No. 1)Publication Date: 2014-03-01
Authors : Parinaz Ghadam; Rana Samadi;
Page : 1-8
Keywords : DNA binding proteins; Histone-like protein; HBsu; HU; Halobacillus karajensis;
Abstract
The histone-like protein HU is the most-abundant DNA-binding protein in bacteria. The HU protein non-specifically binds and bends DNA as a hetero- or homodimer, and can participate in DNA supercoiling and DNA condensation. It also takes part in DNA functions such as replication, recombination, and repair. HU does not recognize any specific sequences but shows a certain degree of specificity to cruciform DNA and repair intermediates such as nick, gap, bulge, etc. To understand the features of HU binding to DNA and repair intermediates, a fast and easy HU protein purification method is required. Here we report a two-step purification procedure of HU from Halobacillus karajensis (the gram positive and moderately halophilic bacteria isolated from Karaj surface soil). The method of HU purification allows obtaining a pure non-tagged protein. Salting out and ion exchange chromatography were applied for purification, and the purified protein was identified by immunoblotting. Results showed that the molecular weight of the purified protein was approximately 11 kDa which is immunologically similar to the Bacillus subtilis HU protein (HBsu).
Other Latest Articles
- Phylogenetic analysis of Persian Gazella, Gazella subgutturosa (Artiodactyla: Bovidae) based on cytochrome b in central Iran
- Phylogenetic analysis of Escherichia coli strains isolated from human samples
- The biometric and cytochrome oxidase subunit I (COI) gene sequence analysis of syngnathus abaster (Teleostei: Syngnathidae) in Caspian sea
- The effect of pH on recombinant C-terminal domain of Botulinum Neurotoxin type E (rBoNT/E-HCC)
- Mechanistic prospective for human PrPC conversion to PrPSc: Molecular dynamic insights
Last modified: 2015-04-25 15:11:36