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( Rajkrishna Mondal ),( Palas K Chanda ),( Amitava Bandhu ),( Biswanath Jana ),( Chia Y Lee ),( Subrata Sau ) 생화학분자생물학회 (구 한국생화학분자생물학회) 2010 BMB Reports Vol.43 No.7
Previously, various inhibitors of cell wall synthesis induced the drp35 gene of Staphylococcus aureus efficiently. To determine whether drp35 could be exploited in antistaphylococcal drug discovery, we cloned the promoter of drp35 (Pd) and developed different biological assay systems using an engineered S. aureus strain that harbors a chromosomally-integrated Pd - lacZ transcriptional fusion. An agarose-based assay showed that Pd is induced not only by the cell wall-affecting antibiotics but also by rifampicin and ciprofloxacin. In contrast, a liquid medium- based assay revealed the induction of Pd specifically by the cell wall-affecting antibiotics. Induction of Pd by sublethal concentrations of cell wall-affecting antibiotics was even assessable in a microtiter plate assay format, indicating that this assay system could be potentially used for high-throughput screening of new cell wall-inhibiting compounds. [BMB reports 2010; 43(7): 468-473]
Stabilization of the primary sigma factor of Staphylococcus aureus by core RNA polymerase
( Rajkrishna Mondal ),( Tridib Ganguly ),( Palas K Chanda ),( Amitava Bandhu ),( Biswanath Jana ),( Keya Sau ),( Chia Y Lee ),( Subrata Sau ) 한국생화학분자생물학회 (구 한국생화학회) 2010 BMB Reports Vol.43 No.3
The primary sigma factor (σA) of Staphylococcus aureus, a potential drug target, was little investigated at the structural level. Using an N-terminal histidine-tagged σA (His-σA), here we have demonstrated that it exits as a monomer in solution, possesses multiple domains, harbors primarily α-helix and efficiently binds to a S. aureus promoter DNA in the presence of core RNA polymerase. While both N- and C-terminal ends of His- σA are flexible in nature, two Trp residues in its DNA binding region are buried. Upon increasing the incubation temperature from 25° to 40℃, ~60% of the input His-σA was cleaved by thermolysin. Aggregation of His-σA was also initiated rapidly at 45℃. From the equilibrium unfolding experiment, the Gibbs free energy of stabilization of His-σA was estimated to be +0.70 kcal mol-1. The data together suggest that primary sigma factor of S. aureus is an unstable protein. Core RNA polymerase however stabilized σA appreciably. [BMB reports 2010; 43(3): 176-181]