Structural plasticity of the Salmonella FliS flagellar export chaperone
Structural plasticity of the Salmonella FliS flagellar export chaperone
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DOI：
10.1002/1873-3468.12149
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发表时间：
2016-04-01
期刊：
影响因子：
3.5
通讯作者：
Vonderviszt, Ferenc
中科院分区：
文献类型：
--
作者：
Sajo, Rachel;Toke, Orsolya;Vonderviszt, Ferenc
弗氏沙门氏菌鞭毛出口伴侣蛋白是一种高度螺旋的蛋白质。蛋白质分解实验表明，Flis具有致密的核心。然而，FIIS的量热熔化轮廓在25-110摄氏度的温度范围内没有显示任何熔化转变。圆二色谱测量表明，在加热时，Flis在很大的温度范围内失去了螺旋结构。这些观察表明，Flis以非合作的方式展开，其自然状态显示出使人想起具有实质性结构可塑性的蛋白质的熔融球状状态的特征。由于Flis在细胞内有几个结合伙伴，构象适应性似乎是履行其多重角色的基本要求。
The Salmonella FliS flagellar export chaperone is a highly -helical protein. Proteolytic experiments suggest that FliS has a compact core. However, the calorimetric melting profile of FliS does not show any melting transition in the 25-110 degrees C temperature range. Circular dichroism measurements reveal that FliS is losing its helical structure over a broad temperature range upon heating. These observations indicate that FliS unfolds in a noncooperative way and its native state shows features reminiscent of the molten globule state of proteins possessing substantial structural plasticity. As FliS has several binding partners within the cell, conformational adaptability seems to be an essential requirement to fulfill its multiple roles.