State Key Laboratory of Medical Molecular Biology, Department of Microbiology and Parasitology, Institute of Basic Medical Sciences Chinese Academy of Medical Sciences, School of Basic Medicine Peking Union Medical College, 100005, Beijing, China.
Institute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Stefan-Meier-Straße 17, 79104, Freiburg im Breisgau, Germany.
Biochem Biophys Res Commun. 2021 May 7;552:73-77. doi: 10.1016/j.bbrc.2021.03.043. Epub 2021 Mar 17.
The biogenesis of outer membrane proteins requires the function of β-barrel assembly machinery (BAM), whose function is highly conserved while its composition is variable. The Escherichia coli BAM is composed of five subunits, while Thermus thermophilus seems to contain a single BAM protein, named TtOmp85. To search for the primitive form of a functional BAM, we investigated and compared the function of TtOmp85 and E. coli BAM by use of a reconstitution assay that examines the integration of OmpA and BamA from E. coli and TtoA from T. thermophilus, as well as the translocation of the E. coli Ag43. Our results show that a single TtOmp85 protein can substitute for the collective function of the five subunits constituting E. coli BAM.
外膜蛋白的生物发生需要β-桶组装机制（BAM）的功能，其功能高度保守，而其组成则是可变的。大肠杆菌的 BAM 由五个亚基组成，而嗜热球菌似乎只含有一种 BAM 蛋白，称为 TtOmp85。为了寻找具有功能的 BAM 的原始形式，我们通过重组测定法研究和比较了 TtOmp85 和大肠杆菌 BAM 的功能，该测定法检查了来自大肠杆菌的 OmpA 和 BamA 以及来自嗜热球菌的 TtoA 的整合，以及大肠杆菌 Ag43 的易位。我们的结果表明，单个 TtOmp85 蛋白可以替代大肠杆菌 BAM 的五个亚基的集体功能。
