Linked domain architectures allow for specialization of function in the FtsK/SpoIIIE ATPases of ESX secretion systems.
Linked domain architectures allow for specialization of function in the FtsK/SpoIIIE ATPases of ESX secretion systems.
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DOI：
10.1016/j.jmb.2014.06.013
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发表时间：
2015-03-13
影响因子：
5.6
通讯作者：
Burton, Briana M.
中科院分区：
文献类型：
--
作者：
Ramsdell, Talia L.;Huppert, Laura A.;Sysoeva, Tatyana A.;Fortune, Sarah M.;Burton, Briana M.
关键词：
在蛋白质分泌系统中，有专门的ATP酶，它们具有不同的功能，如底物识别、底物解折叠和分泌机制的组装。ESX蛋白分泌系统需要FtsK/SpoIIIE家族ATP酶，但这些ATP酶的具体功能知之甚少。ESX分泌系统的ATP酶在FtsK/SpoIIIE家族的蛋白质中具有独特的结构域结构。迄今为止，所有研究充分的FtsK家族ATP酶都具有一个ATP酶结构域，并寡聚形成功能性分子机器，最常见的是六聚环。相比之下，ESX ATP酶具有三个ATP酶结构域，由单个基因或两个操纵子基因编码。目前尚不清楚哪个ATP酶结构域具有催化功能，以及每个结构域是否发挥相同或不同的功能。在这里，我们重点研究了两个ESX系统的ATP酶，即结核分枝杆菌的ESX-1系统和枯草杆菌的yuk系统。我们表明，ATP水解的ESX ATP酶是必需的分泌，这表明这种酶至少部分燃料蛋白质易位。我们进一步表明，个别ATP酶结构域发挥不同的作用，在底物转运和复合物的形成。比较单链和分裂的ESX ATP酶，我们揭示了这些独特的分泌型ATP酶的要求的差异。
Among protein secretion systems there are specialized ATPases that serve different functions such as substrate recognition, substrate unfolding, and assembly of the secretory machinery. ESX protein secretion systems require FtsK/SpoIIIE family ATPases but the specific function of these ATPases is poorly understood. The ATPases of ESX secretion systems have a unique domain architecture among proteins of the FtsK/SpoIIIE family. All well-studied FtsK family ATPases to date have one ATPase domain and oligomerize to form a functional molecular machine, most commonly a hexameric ring. In contrast, the ESX ATPases have three ATPase domains, either encoded by a single gene or by two operonic genes. It is currently unknown which of the ATPase domains is catalytically functional and whether each domain plays the same or a different function. Here we focus on the ATPases of two ESX systems, the ESX-1 system of Mycobacterium tuberculosis and the yuk system of Bacillus subtilis. We show that ATP hydrolysis by the ESX ATPase is required for secretion, suggesting that this enzyme at least partly fuels protein translocation. We further show that individual ATPase domains play distinct roles in substrate translocation and complex formation. Comparing the single chain and split ESX ATPases we reveal differences in the requirements of these unique secretory ATPases.
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影响因子：
3
作者：
Huyton, T;Pye, VE;Freemont, PS
通讯作者：
Freemont, PS
DOI：
10.1073/pnas.1119453109
发表时间：
2012-07-10
影响因子：
11.1
作者：
Daleke, Maria H.;Ummels, Roy;Bitter, Wilbert
通讯作者：
Bitter, Wilbert
影响因子：
2.1
作者：
Fujita, M
通讯作者：
Fujita, M
DOI：
10.1073/pnas.0504922102
发表时间：
2005-07-26
影响因子：
11.1
作者：
Fortune, SM;Jaeger, A;Rubin, EJ
通讯作者：
Rubin, EJ
影响因子：
3.6
作者：
Guinn, KM;Hickey, MJ;Sherman, DR
通讯作者：
Sherman, DR