Nomenclature Abstract for Bacillus thermoglucosidasius Suzuki et al. 1984.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Nicole Danielle Osier ◽  
George M Garrity
1983 ◽  
Vol 4 (4) ◽  
pp. 487-495 ◽  
Author(s):  
Yuzuru Suzuki ◽  
Takashi Kishigami ◽  
Kiyoshi Inoue ◽  
Yasuhiro Mizoguchi ◽  
Nobuyuki Eto ◽  
...  

2001 ◽  
Vol 183 (1) ◽  
pp. 155-161 ◽  
Author(s):  
Kunihiko Watanabe ◽  
Takeshi Yamamoto ◽  
Yuzuru Suzuki

ABSTRACT HrcA, a negative control repressor for chaperone expression from the obligate thermophile Bacillus thermoglucosidasiusKP1006, was purified in a His-tagged form in the presence of 6 M urea but hardly renatured to an intact state due to extreme insolubility. Renaturation trials revealed that the addition of DNA to purifiedB. thermoglucosidasius HrcA can result in solubilization of HrcA free from the denaturing agent urea. Results from band shift and light scattering assays provided three new findings: (i) any species of DNA can serve to solubilize B. thermoglucosidasius HrcA, but DNA containing the CIRCE (controlling inverted repeat of chaperone expression) element is far more effective than other nonspecific DNA; (ii) B. thermoglucosidasius HrcA renatured with nonspecific DNA bound the CIRCE element in the molecular ratio of 2.6:1; and (iii)B. thermoglucosidasius HrcA binding to the CIRCE element was stable at below 50°C whereas the complex was rapidly denatured at 70°C, suggesting that the breakdown of HrcA is induced by heat stress and HrcA may act as a thermosensor to affect the expression of heat shock regulatory genes. These results will help to determine the nature of HrcA protein molecules.


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