Leusenko Anna V, Mironov Kirill S, Los Dmitry A
K.A. Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Botanicheskaya Street 35, Moscow, 127276, Russia.
K.A. Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Botanicheskaya Street 35, Moscow, 127276, Russia.
Biochimie. 2024 Mar;218:76-84. doi: 10.1016/j.biochi.2023.08.004. Epub 2023 Aug 9.
The PAS (Per-ARNT-Sim) domain is a sensory protein regulatory module found in archaea, prokaryotes, and eukaryotes. Histidine and serine/threonine protein kinases, chemo- and photoreceptors, circadian rhythm regulators, ion channels, phosphodiesterases, and other cellular response regulators are among these proteins. Hik33 is a multifunctional sensory histidine kinase that is implicated in cyanobacterial responses to cold, salt, hyperosmotic, and oxidative stressors. The functional roles of individual Hik33 domains in signal transduction were investigated in this study. Synechocystis Hik33 deletion variants were developed, in which either both or a portion of the transmembrane domains and/or the PAS domain were deleted. Cold stress was applied to the mutant strains either under illumination or in the dark. The findings show that the transmembrane domains govern temperature responses, whereas PAS domain may be involved in regulation of downstream gene expression in light-dependent manner.
PAS（Per-ARNT-Sim）结构域是一种在古细菌、原核生物和真核生物中发现的传感蛋白调节模块。这些蛋白质包括组氨酸和丝氨酸/苏氨酸蛋白激酶、化学感受器和光感受器、昼夜节律调节因子、离子通道、磷酸二酯酶以及其他细胞反应调节因子。Hik33是一种多功能传感组氨酸激酶，与蓝细菌对寒冷、盐、高渗和氧化应激源的反应有关。本研究调查了单个Hik33结构域在信号转导中的功能作用。构建了集胞藻Hik33缺失变体，其中跨膜结构域的全部或部分和/或PAS结构域被删除。在光照或黑暗条件下对突变菌株施加冷应激。研究结果表明，跨膜结构域控制温度反应，而PAS结构域可能以光依赖的方式参与下游基因表达的调节。
