Nakano M M, Zhu Y
Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Beaverton, Oregon 97006, USA.
J Bacteriol. 2001 Mar;183(6):1938-44. doi: 10.1128/JB.183.6.1938-1944.2001.
The ResD-ResE signal transduction system is required for aerobic and anaerobic respiration in Bacillus subtilis. The histidine sensor kinase ResE, by functioning as a kinase and a phosphatase for the cognate response regulator ResD, controls the level of phosphorylated ResD. A high level of phosphorylated ResD is postulated to cause a dramatic increase in transcription of ResDE-controlled genes under anaerobic conditions. A mutant ResE, which retains autophosphorylation and ResD phosphorylation activities but is defective in ResD dephosphorylation, allowed partially derepressed aerobic expression of the ResDE-controlled genes. The result indicates that phosphatase activity of ResE is regulated by oxygen availability and anaerobic induction of the ResDE regulon is partly due to a reduction of the ResE phosphatase activity during anaerobiosis. That elimination of phosphatase activity does not result in complete aerobic derepression suggests that the ResE kinase activity is also subject to control in response to oxygen limitation.
ResD-ResE信号转导系统是枯草芽孢杆菌有氧呼吸和无氧呼吸所必需的。组氨酸传感器激酶ResE通过作为同源应答调节因子ResD的激酶和磷酸酶发挥作用,控制磷酸化ResD的水平。据推测,在厌氧条件下,高水平的磷酸化ResD会导致ResDE控制基因的转录显著增加。一种突变的ResE,它保留了自身磷酸化和ResD磷酸化活性,但在ResD去磷酸化方面存在缺陷,使得ResDE控制基因的需氧表达部分去阻遏。结果表明,ResE的磷酸酶活性受氧气可用性调节,ResDE操纵子的厌氧诱导部分归因于厌氧期间ResE磷酸酶活性的降低。磷酸酶活性的消除并未导致完全的需氧去阻遏,这表明ResE激酶活性也会响应氧气限制而受到调控。