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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]
Ganguly, Tridib,Chattoraj, Partho,Das, Malabika,Chanda, Palas K.,Mandal, Nitai.C.,Lee, Chia Y.,Sau, Subrata Korean Society for Biochemistry and Molecular Biol 2004 Journal of biochemistry and molecular biology Vol.37 No.6
The wild-type repressor CI of temperate mycobacteriophage L1 and the temperature-sensitive (ts) repressor CIts391 of a mutant L1 phage, L1cIts391, have been separately overexpressed in E. coli. Both these repressors were observed to specifically bind with the same cognate operator DNA. The operator-binding activity of CIts391 was shown to differ significantly than that of the CI at 32 to $42^{\circ}C$. While 40-95% operator-binding activity was shown to be retained at 35 to $42^{\circ}C$ in CI, more than 75% operator-binding activity was lost in CIts391 at 35 to $38^{\circ}C$, although the latter showed only 10% less binding compared to that of the former at $32^{\circ}C$. The CIts391 showed almost no binding at $42^{\circ}C$. An in vivo study showed that the CI repressor inhibited the growth of a clear plaque former mutant of the L1 phage more strongly than that of the CIts391 repressor at both 32 and $42^{\circ}C$. The half-life of the CIts391-operator complex was found to be about 8 times less than that of the CI-operator complex at $32^{\circ}C$. Interestingly, the repressor-operator complexes preformed at $0^{\circ}C$ have shown varying degrees of resistance to dissociation at the temperatures which inhibit the formation of these complexes are inhibited. The CI repressor, but not that of CIts391, regains most of the DNA-binding activity on cooling to $32^{\circ}C$ after preincubation at 42 to $52^{\circ}C$. All these data suggest that the 131st proline residue at the C-terminal half of CI, which changed to leucine in the CIts391, plays a crucial role in binding the L1 repressor to the cognate operator DNA, although the helix-turn-helix DNA-binding motif of the L1 repressor is located at its N-terminal end.
( Tridib Ganguly ),( Partho Chattoraj ),( Malabika Das ),( Palas K. Chanda ),( Nitai. C. Mandal ),( Chia Y. Lee ),( Subrata Sau ) 생화학분자생물학회 2004 BMB Reports Vol.37 No.6
The wild-type repressor CI of temperate mycobacteriophage Ll and the temperature-sensitive (ts) repressor CIts391 of a mutant Ll phage, LlcIts391, have been separately overexpressed in E. coli. Both these repressors were observed to specifically bind with the same cognate operator DNA. The operator-binding activity of CIts391 was shown to differ significantly than that of the CI at 32 to 42C. While 40-95% operator-binding activity was shown to be retained at 35 to 42C in CI, more than 75% operator-binding activity was lost in CIts391 at 35 to 38℃, although the latter showed only 10% less binding compared to that of the former at 32℃. The CIts391 showed almost no binding at 42℃. An in vivo study showed that the CI repressor inhibited the growth of a clear plaque former mutant of the L1 phage more strongly than that of the CIts391 repressor at both 32 and 42℃. The half-life of the CIts391-operator complex was found to be about 8 times less than that of the CI-operator complex at 32C. Interestingly, the repressor-operator complexes preformed at 0C have shown varying degrees of resistance to dissociation at the temperatures which inhibit the formation of these complexes are inhibited. The CI repressor, but not that of CIts391, regains most of the DNA-binding activity on cooling to 32C after preincubation at 42 to 52C. All these data suggest that the 131 proline residue at the C-terminal half of CI, which changed to leucine in the CIts391, plays a crucial role in binding the L1 repressor to the cognate operator DNA, although the helix-turn-helix DNA-binding motif of the LI repressor is located at its N-terminal end.