共查询到20条相似文献,搜索用时 62 毫秒
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Sheng-Chia Chen Chi-Fon Chang Pei-Ju Fan Ya-Hsin Cheng Tsunai Yu Tai-huang Huang 《Biomolecular NMR assignments》2013,7(1):85-88
Bacterial cells often use two-component signal transduction systems to regulate genes in response to environmental stimuli. The RstA/RstB system is a two-component regulatory system consisting of the membrane sensor, RstB, and its cognate response regulator RstA. The RstA of Klebsiella pneumoniae consists of a N-terminal receiver domain (NRD, residues 1-119) and a C-terminal DNA-binding domain (DBD, residues 130-236). Phosphorylation of the response regulator induces a conformational change in the regulatory domain of RstA, which results in activation of the effector domain to regulate the downstream genes, including the ferrous iron transport system (Feo), at low-pH condition. Here we report the 1H, 13C and 15N resonance assignments and secondary structure identification of the DBD of RstA from K. pneumoniae as a first step for unraveling the structural and functional relationship of the RstA/RstB two component system. 相似文献
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Yi-Chuan Li Chung-ke Chang Chi-Fon Chang Ya-Hsin Cheng Pei-Ju Fang Tsunai Yu Sheng-Chia Chen Yi-Ching Li Chwan-Deng Hsiao Tai-huang Huang 《Nucleic acids research》2014,42(13):8777-8788
The RstA/RstB system is a bacterial two-component regulatory system consisting of the membrane sensor, RstB and its cognate response regulator (RR) RstA. The RstA of Klebsiella pneumoniae (kpRstA) consists of an N-terminal receiver domain (RD, residues 1–119) and a C-terminal DNA-binding domain (DBD, residues 130–236). Phosphorylation of kpRstA induces dimerization, which allows two kpRstA DBDs to bind to a tandem repeat, called the RstA box, and regulate the expression of downstream genes. Here we report the solution and crystal structures of the free kpRstA RD, DBD and DBD/RstA box DNA complex. The structure of the kpRstA DBD/RstA box complex suggests that the two protomers interact with the RstA box in an asymmetric fashion. Equilibrium binding studies further reveal that the two protomers within the kpRstA dimer bind to the RstA box in a sequential manner. Taken together, our results suggest a binding model where dimerization of the kpRstA RDs provides the platform to allow the first kpRstA DBD protomer to anchor protein–DNA interaction, whereas the second protomer plays a key role in ensuring correct recognition of the RstA box. 相似文献
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Chen CC Ghole M Majumder A Wang Z Chandana S Wu HY 《The Journal of biological chemistry》2003,278(39):38094-38103
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Positive and negative regulation of the cardiovascular transcription factor KLF5 by p300 and the oncogenic regulator SET through interaction and acetylation on the DNA-binding domain 下载免费PDF全文
Miyamoto S Suzuki T Muto S Aizawa K Kimura A Mizuno Y Nagino T Imai Y Adachi N Horikoshi M Nagai R 《Molecular and cellular biology》2003,23(23):8528-8541
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Xiaohong Zhou Zhiyong Lou Sheng Fu Anqi Yang Zexuan Li Mark Bartlam Zihe Rao 《Journal of molecular biology》2010,396(4):1012-1024