The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lα
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lα
复制标题
DOI：
10.1093/emboj/19.17.4493
复制
发表时间：
2000-09-01
期刊：
影响因子：
11.4
通讯作者：
Braakman, I
中科院分区：
文献类型：
--
作者：
Benham, AM;Cabibbo, A;Braakman, I
正确形成的二硫键的存在对于在内质网（ER）中合成的蛋白质的结构和功能至关重要，二硫键的形成在ER中发生，这是由于存在几种专门的催化剂和合适的氧化还原电位，在酵母中的工作已经表明，ER驻留糖蛋白Ero 1 p通过蛋白质二硫键异构酶（PDI）为新合成的蛋白质提供氧化等价物。在这里，我们表明，Ero 1-L α，Ero 1 p的人类同源物，存在作为一个集合的氧化和还原形式和共价结合PDI。我们分析了假定活性位点C（391）VGCFKC（397）中的Ero 1-L α半胱氨酸突变体。我们的结果表明，该基序对于Ero 1-L alpha-PDI复合物的蛋白质折叠、结构完整性、蛋白质半衰期和稳定性非常重要。
The presence of correctly formed disulfide bonds is crucial to the structure and function of proteins that are synthesized in the endoplasmic reticulum (ER), Disulfide bond formation occurs in the ER owing to the presence of several specialized catalysts and a suitable redox potential, Work in yeast has indicated that the ER resident glycoprotein Ero1p provides oxidizing equivalents to newly synthesized proteins via protein disulfide isomerase (PDI). Here we show that Ero1-L alpha, the human homolog of Ero1p, exists as a collection of oxidized and reduced forms and covalently binds PDI. We analyzed Ero1-L alpha cysteine mutants in the presumed active site C(391)VGCFKC(397). Our results demonstrate that this motif is important for protein folding, structural integrity, protein half-life and the stability of the Ero1-L alpha-PDI complex.