The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
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DOI：
10.1093/emboj/16.21.6394
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发表时间：
1997-11-03
期刊：
影响因子：
11.4
通讯作者：
Hultgren, SJ
中科院分区：
文献类型：
--
作者：
Jones, CH;Danese, PN;Hultgren, SJ
相互作用的蛋白质亚基组装成胞外结构，如肠杆菌科中的菌毛纤维，依赖于PapD样周质伴侣的活性。PapD与菌毛亚基的疏水性C-末端进行β拉链相互作用的能力促进它们从细胞质膜折叠和释放到周质中。在没有分子伴侣的情况下，亚基仍然被束缚在膜上，并通过非生产性相互作用被驱动离开通路。这些非途径反应对细胞生长是有害的;野生型生长通过PapD的共表达而恢复。在PapD缺失的情况下，亚基错误折叠通过两条平行的通路感知：Cpx双组分信号系统和调节通路。
The assembly of interactive protein subunits into extracellular structures, such as pilus fibers in the Enterobacteriaceae, is dependent on the activity of PapD-like periplasmic chaperones. The ability of PapD to undergo a beta zippering interaction with the hydrophobic C-terminus of pilus subunits facilitates their folding and release from the cytoplasmic membrane into the periplasm. In the absence of the chaperone, subunits remained tethered to the membrane and were driven off-pathway via non-productive interactions. These off-pathway reactions were detrimental to cell growth; wild-type growth was restored by co-expression of PapD. Subunit misfolding in the absence of PapD was sensed by two parallel pathways: the Cpx two-component signaling system and the of modulatory pathway.