The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
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DOI：
10.1111/j.1574-6968.1999.tb13650.x
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发表时间：
1999-07-01
影响因子：
2.1
通讯作者：
Ponting, CP
中科院分区：
文献类型：
--
作者：
Aravind, L;Ponting, CP
先前已证明受体组氨酸激酶和化学感受器蛋白的细胞质接头区域的突变会显着损害受体功能。在这里，我们证明了许多组氨酸激酶、甲基接受蛋白、腺苷酸环化酶和其他原核信号蛋白中这些区域之间的显着序列相似性。研究表明，这些“HAMP 结构域”通过将周质配体结合结构域的构象变化传递给细胞质信号激酶和甲基受体结构域，具有调节同型二聚体受体磷酸化或甲基化的作用。 (C) 1999 年由 Elsevier Science B.V. 出版。保留所有权利。
Mutations in the cytoplasmic linker regions of receptor histidine kinase and chemoreceptor proteins have been shown previously to significantly impair receptor functions. Here we demonstrate significant sequence similarities between these regions in numerous histidine kinases, methyl-accepting proteins, adenylyl cyclases and other prokaryotic signalling proteins. It is suggested that these 'HAMP domains' possess roles of regulating the phosphorylation or methylation of homodimeric receptors by transmitting the conformational changes in periplasmic ligand-binding domains to cytoplasmic signalling kinase and methyl-acceptor domains. (C) 1999 Published by Elsevier Science B.V. All rights reserved.