期刊
OPEN BIOLOGY
卷 4, 期 6, 页码 -出版社
ROYAL SOC
DOI: 10.1098/rsob.140023
关键词
DctB; two-component system; transmembrane signal transduction
资金
- 973 National Key Basic Research Program in China [2010CB126503]
- NSFC of People's Republic of China [30830005, 30728002, 30870030]
- Program of Introducing Talents of Discipline to Universities [B06001]
- State Key Laboratory of Protein and Plant Gene Research [B02]
- National Science Fund for Distinguished Young Scholars (NSFC) [39925017]
Membrane-associated histidine kinases (HKs) in two-component systems respond to environmental stimuli by autophosphorylation and phospho-transfer. HK typically contains a periplasmic sensor domain that regulates the cytoplasmic kinase domain through a conserved cytoplasmic linker. How signal is transduced from the ligand-binding site across the membrane barrier remains unclear. Here, we analyse two linker regions of a typical HK, DctB. One region connects the first transmembrane helix with the periplasmic Per-ARNT-Sim domains, while the other one connects the second transmembrane helix with the cytoplasmic kinase domains. We identify a leucine residue in the first linker region to be essential for the signal transduction and for maintaining the delicate balance of the dimeric interface, which is key to its activities. We also show that the other linker, belonging to the S-helix coiled-coil family, plays essential roles in signal transduction inside the cell. Furthermore, by combining mutations with opposing activities in the two regions, we show that these two signalling transduction elements are integrated to produce a combined effect on the final activity of DctB.
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