Mammalian PASKIN, a PAS-serine/threonine kinase related to bacterial oxygen sensors
Mammalian PASKIN, a PAS-serine/threonine kinase related to bacterial oxygen sensors
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DOI：
10.1006/bbrc.2001.5840
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发表时间：
2001-11-09
影响因子：
3.1
通讯作者：
Wenger, RH
中科院分区：
文献类型：
--
作者：
Hofer, T;Spielmann, P;Wenger, RH
PAS结构域是在许多古细菌、细菌和植物蛋白中发现的多用途蛋白折叠，能够感知光强度、氧浓度和氧化还原电位等环境变化。来自根瘤菌物种的氧传感器FixL包含一个含血红素的PAS结构域和一个组氨酸激酶结构域，该结构域将传感与信号传导偶联。我们鉴定了一种新的哺乳动物PAS蛋白（PASKIN），其结构域类似于FixL。PASKIN是由一个进化上保守的单拷贝基因编码的，该基因普遍表达。人类和小鼠PASKIN基因显示保守的内含子结构，并与另一个普遍表达的编码蛋白磷酸酶-1调节因子的基因共享其启动子区域。144 kda的PASKIN蛋白包含一个与FixL PAS结构域同源的PAS区域和一个可能参与信号传导的丝氨酸/苏氨酸激酶结构域。因此，PASKIN可能具有哺乳动物PAS传感器蛋白的功能。(C) 2001学术出版社。
The PAS domain is a versatile protein fold found in many archaeal, bacterial, and plant proteins capable of sensing environmental changes in light intensity, oxygen concentration, and redox potentials. The oxygen sensor FixL from Rhizobium species contains a heme-bearing PAS domain and a histidine kinase domain that couples sensing to signaling. We identified a novel mammalian PAS protein (PASKIN) containing a domain architecture resembling FixL. PASKIN is encoded by an evolutionarily conserved single-copy gene which is ubiquitously expressed. The human PASKIN and mouse Paskin genes show a conserved intronexon structure and share their promoter regions with another ubiquitously expressed gene that encodes a regulator of protein phosphatase-1. The 144-kDa PASKIN protein contains a PAS region homologous to the FixL PAS domain and a serine/threonine kinase domain which might be involved in signaling. Thus, PASKIN is likely to function as a mammalian PAS sensor protein. (C) 2001 Academic Press.