Stabilization of the primary sigma factor of Staphylococcus aureus by core RNA polymerase.
Stabilization of the primary sigma factor of Staphylococcus aureus by core RNA polymerase.
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DOI:
10.5483/bmbrep.2010.43.3.176
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发表时间:
2010-03
期刊:
影响因子:
3.8
通讯作者:
Sau S
中科院分区:
文献类型:
--
作者:
Mondal R;Ganguly T;Chanda PK;Bandhu A;Jana B;Sau K;Lee CY;Sau S
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 Nand C-terminal ends of HisσA are flexible in nature, two Trp residues in its DNA binding region are buried. Upon increasing the incubation temperature from 25° to 40°C, ~60% of the input His-σA was cleaved by thermolysin. Aggregation of His-σA was also initiated rapidly at 45oC. 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]
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影响因子:
12.3
作者:
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通讯作者:
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影响因子:
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作者:
Ganguly, Tridib;Bandhu, Amitava;Sau, Subrata
通讯作者:
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DOI:
10.1006/bbrc.1995.1382
发表时间:
1995-03-17
影响因子:
3.1
作者:
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通讯作者:
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影响因子:
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影响因子:
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作者:
Ganguly, Tridib;Das, Malabika;Sau, Subrata
通讯作者:
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