阴离子脂质调节水甘油通道蛋白GlpF的活性。
Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF.
作者信息
Klein Noreen, Hellmann Nadja, Schneider Dirk
机构信息
Institut für Pharmazie und Biochemie, Johannes Gutenberg Universität Mainz, Mainz, Germany.
Institut für Molekulare Biophysik, Johannes Gutenberg Universität Mainz, Mainz, Germany.
出版信息
Biophys J. 2015 Aug 18;109(4):722-31. doi: 10.1016/j.bpj.2015.06.063.
The structure and composition of a biological membrane can severely influence the activity of membrane-embedded proteins. Here, we show that the E. coli aquaglyceroporin GlpF has only little activity in lipid bilayers formed from native E. coli lipids. Thus, at first glance, GlpF appears to not be optimized for its natural membrane environment. In fact, we found that GlpF activity was severely affected by negatively charged lipids regardless of the exact chemical nature of the lipid headgroup, whereas GlpF was not sensitive to changes in the lateral membrane pressure. These observations illustrate a potential mechanism by which the activity of an α-helical membrane protein is modulated by the negative charge density around the protein.
生物膜的结构和组成会严重影响膜嵌入蛋白的活性。在此，我们表明大肠杆菌水甘油通道蛋白GlpF在由天然大肠杆菌脂质形成的脂质双层中活性很低。因此，乍一看，GlpF似乎并未针对其天然膜环境进行优化。事实上，我们发现无论脂质头基团的确切化学性质如何，带负电荷的脂质都会严重影响GlpF的活性，而GlpF对侧向膜压力的变化不敏感。这些观察结果说明了一种潜在机制，即α-螺旋膜蛋白的活性是如何由蛋白周围的负电荷密度调节的。
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