Hemilä H, Palva A, Paulin L, Adler L, Arvidson S, Palva I
Institute of Biotechnology, Helsinki.
Res Microbiol. 1991 Sep-Oct;142(7-8):779-85. doi: 10.1016/0923-2508(91)90055-f.
We have cloned the operon for the Bacillus subtilis S complex, which has been suggested to be a component of the protein secretion machinery. The S-complex operon was found to encode 4 proteins, which were identified as subunits of pyruvate dehydrogenase (PDH). The Staphylococcus aureus membrane-bound ribosome protein (MBRP) complex has been considered to be a counterpart of the B. subtilis S complex. Here, we sequenced a fragment of the MBRP operon encoding the C-terminal part of E1 beta, the entire E2 and the N-terminal part of the E3 subunit of PDH, thus conclusively confirming the PDH identity of the MBRP complex as well. It appeared unlikely that PDH could be a primary component in protein secretion, thus disproving the previous hypothesis of the role of the S complex. However, attachment of the S complex (PDH) to the membrane and ribosomes may produce a biologically significant interaction.
我们克隆了枯草芽孢杆菌S复合物的操纵子，该复合物被认为是蛋白质分泌机制的一个组成部分。发现S复合物操纵子编码4种蛋白质，它们被鉴定为丙酮酸脱氢酶（PDH）的亚基。金黄色葡萄球菌膜结合核糖体蛋白（MBRP）复合物被认为是枯草芽孢杆菌S复合物的对应物。在这里，我们对编码PDH的E1β亚基C末端部分、整个E2亚基和E3亚基N末端部分的MBRP操纵子片段进行了测序，从而最终证实了MBRP复合物也具有PDH的特性。PDH似乎不太可能是蛋白质分泌的主要成分，从而推翻了之前关于S复合物作用的假设。然而，S复合物（PDH）与膜和核糖体的附着可能会产生具有生物学意义的相互作用。
