Kim Y J, Oliver D B
Department of Molecular Biology and Biochemistry, Wesleyan University, Middletown, CT 06459.
FEBS Lett. 1994 Feb 14;339(1-2):175-80. doi: 10.1016/0014-5793(94)80410-9.
In order to test whether SecY and SecE proteins constitute the SecA receptor inside out membrane vesicles where prepared from strains producing greatly different levels of these two proteins, and their SecA binding activity was quantitated. Substantial overproduction of SecE or SecY and SecE proteins resulted in no increase or only 50% increase, respectively, in the number of high affinity SecA binding sites. These results suggest that SecY and SecE proteins appear insufficient to constitute the primary SecA receptor. The existence of a cycle of SecA association with the inner membrane and its modulation by particular integral membrane proteins is discussed.
为了检测SecY和SecE蛋白是否在由产生这两种蛋白水平差异极大的菌株制备的内膜囊泡中构成了SecA的内向型受体，对它们的SecA结合活性进行了定量分析。大量过量表达SecE或SecY和SecE蛋白分别导致高亲和力SecA结合位点数量没有增加或仅增加50%。这些结果表明，SecY和SecE蛋白似乎不足以构成主要的SecA受体。文中讨论了SecA与内膜结合的循环及其受特定整合膜蛋白调节的情况。
