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An evolutionarily conserved iron-sulfur cluster underlies redox sensory function of the Chloroplast Sensor Kinase.
Communications Biology ( IF 5.2 ) Pub Date : 2020-01-08 , DOI: 10.1038/s42003-019-0728-4
Iskander M Ibrahim 1 , Huan Wu 1 , Roman Ezhov 2 , Gilbert E Kayanja 1 , Stanislav D Zakharov 3 , Yanyan Du 1, 4 , Weiguo Andy Tao 1 , Yulia Pushkar 2 , William A Cramer 3 , Sujith Puthiyaveetil 1
Affiliation  

Photosynthetic efficiency depends on equal light energy conversion by two spectrally distinct, serially-connected photosystems. The redox state of the plastoquinone pool, located between the two photosystems, is a key regulatory signal that initiates acclimatory changes in the relative abundance of photosystems. The Chloroplast Sensor Kinase (CSK) links the plastoquinone redox signal with photosystem gene expression but the mechanism by which it monitors the plastoquinone redox state is unclear. Here we show that the purified Arabidopsis and Phaeodactylum CSK and the cyanobacterial CSK homologue, Histidine kinase 2 (Hik2), are iron-sulfur proteins. The Fe-S cluster of CSK is further revealed to be a high potential redox-responsive [3Fe-4S] center. CSK responds to redox agents with reduced plastoquinone suppressing its autokinase activity. Redox changes within the CSK iron-sulfur cluster translate into conformational changes in the protein fold. These results provide key insights into redox signal perception and propagation by the CSK-based chloroplast two-component system.

中文翻译:

进化上保守的铁硫簇是叶绿体传感器激酶的氧化还原感觉功能的基础。

光合效率取决于两个光谱不同的串联光系统的相等光能转换。位于两个光系统之间的质体醌库的氧化还原状态是​​一个关键的调节信号,它启动了光系统相对丰度的适应性变化。叶绿体传感器激酶(CSK)将质体醌氧化还原信号与光系统基因表达联系起来,但其监测质体醌氧化还原状态的机制尚不清楚。在这里,我们显示纯化的拟南芥和拟杆菌CSK和蓝细菌CSK同源物,组氨酸激酶2(Hik2),是铁硫蛋白。CSK的Fe-S团簇进一步显示是一个高电位的氧化还原反应性[3Fe-4S]中心。CSK响应氧化还原剂减少的塑料醌抑制其自身激酶活性。CSK铁-硫簇内的氧化还原变化转化为蛋白质折叠的构象变化。这些结果为基于CSK的叶绿体两组分系统对氧化还原信号的感知和传播提供了重要的见识。
更新日期:2020-01-08
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