Membrane topology of the N-terminus of the Escherichia coli FtsK division protein
Membrane topology of the N-terminus of the Escherichia coli FtsK division protein
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DOI：
10.1016/s0014-5793(00)01820-2
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发表时间：
2000-07-28
期刊：
影响因子：
3.5
通讯作者：
Dewar, SJ
中科院分区：
文献类型：
--
作者：
Dorazi, R;Dewar, SJ
大肠杆菌FtsK蛋白靶向隔膜，是细胞分裂所必需的，并可能在DNA分配中发挥作用，计算机模拟表明，该蛋白的前180个氨基酸被嵌入细胞质膜中的SIS跨膜结构域，我们证明，使用基因融合，N-末端包含四个跨膜螺旋连接两个周质结构域。第一个周质域含有锌金属蛋白酶的HEXXH氨基酸序列特征，我们通过突变分析表明，HEXXH序列的保守谷氨酸是FtsK功能在分隔过程中必不可少的。(C)2000年欧洲生物化学学会联合会。由Elsevier Science B. V.出版，版权所有。
The Escherichia coli FtsK protein targets the septum, is essential for cell division and may play a role in DNA partitioning, Computer modelling suggests that the first 180 amino acids of the protein are embedded in the cytoplasmic membrane by up to sis transmembrane domains, We demonstrate, using gene fusions, that the N-terminus contains four transmembrane helices that link two periplasmic domains. The first periplasmic domain contains an HEXXH amino acid sequence characteristic of zinc metalloproteases, We show by mutation analysis that the conserved glutamic acid of the HEXXH sequence is essential for FtsK function during septation. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.