Conformational state of the SecYEG-bound SecA probed by single tryptophan fluorescence spectroscopy.
Conformational state of the SecYEG-bound SecA probed by single tryptophan fluorescence spectroscopy.
复制标题
通过单色氨酸荧光光谱探测结合 SecYEG 的 SecA 的构象状态。
作者：
P. Natale;T. den Blaauwen;C. van der Does;A. Driessen
SecYEG复合物是一种膜包埋通道，允许前体蛋白（前蛋白）穿过大肠杆菌的内膜。SecA是与SecYEG孔相关的分子马达，并通过ATP结合和水解的多个循环驱动前蛋白跨膜的逐步易位。我们已经研究了构象状态的可溶性和SecYEG结合SecA使用单色氨酸突变体SecA。SecA的单双链体的荧光光谱性质及其对猝灭剂丙烯酰胺的可接近性表明，SecA经历构象变化，这导致在ATP结合和与SecYEG孔结合时结构更紧凑。此外，SecYEG结合SecA经历了可溶性SecA未观察到的ATP依赖性构象变化。这些数据支持一个模型，其中结合到SecYEG通道上对SecA构象有重大影响。
The SecYEG complex is a membrane-embedded channel that permits the passage of precursor proteins (preproteins) across the inner membrane of Escherichia coli. SecA is a molecular motor that associates with the SecYEG pore and drives the stepwise translocation of preproteins across the membrane through multiple cycles of ATP binding and hydrolysis. We have investigated the conformational state of soluble and SecYEG-bound SecA using single tryptophan mutants of SecA. The fluorescence spectral properties of the single tryptophans of SecA and their accessibility to the quencher acrylamide demonstrate that SecA undergoes a conformational change that results in a more compact structure upon binding of ATP and binding to the SecYEG pore. In addition, SecYEG-bound SecA undergoes ATP-dependent conformational changes that are not observed for soluble SecA. These data support a model in which binding to the SecYEG channel has a major impact on the SecA conformation.
来自大肠杆菌野生型和 SecA51(TS) 突变株的 SecA 蛋白的膜相关和可溶状态的表征。
DOI：
--
发表时间：
1991
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Cabelli,RJ;Dolan,KM;Qian,LP;Oliver,DB
通讯作者：
Oliver,DB
阴离子磷脂和部分解折叠可促进部分大肠杆菌 SecA 蛋白深入渗透到模型膜中。
DOI：
--
发表时间：
1992
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Ulbrandt,ND;London,E;Oliver,DB
通讯作者：
Oliver,DB